Abstract
Actinobacteria is a group of diverse bacteria. Most species in this class of bacteria are filamentous aerobes found in soil, including the genus Streptomyces perhaps best known for their fascinating capabilities of producing antibiotics. These bacteria typically have a Gram-positive cell envelope, comprised of a plasma membrane and a thick peptidoglycan layer. However, there is a notable exception of the Corynebacteriales order, which has evolved a unique type of outer membrane likely as a consequence of convergent evolution. In this chapter, we will focus on the unique cell envelope of this order. This cell envelope features the peptidoglycan layer that is covalently modified by an additional layer of arabinogalactan . Furthermore, the arabinogalactan layer provides the platform for the covalent attachment of mycolic acids , some of the longest natural fatty acids that can contain ~100 carbon atoms per molecule. Mycolic acids are thought to be the main component of the outer membrane, which is composed of many additional lipids including trehalose dimycolate, also known as the cord factor. Importantly, a subset of bacteria in the Corynebacteriales order are pathogens of human and domestic animals, including Mycobacterium tuberculosis. The surface coat of these pathogens are the first point of contact with the host immune system, and we now know a number of host receptors specific to molecular patterns exposed on the pathogen’s surface, highlighting the importance of understanding how the cell envelope of Actinobacteria is structured and constructed. This chapter describes the main structural and biosynthetic features of major components found in the actinobacterial cell envelopes and highlights the key differences between them.
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References
Abou-Zeid C, Voiland A, Michel G, Cocito C (1982) Structure of the wall polysaccharide isolated from a group of corynebacteria. Eur J Biochem 128:363–370
Albesa-Jove D, Svetlikova Z, Tersa M et al (2016) Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA. Nat Commun 7:10906. https://doi.org/10.1038/ncomms10906
Alderwick LJ, Radmacher E, Seidel M et al (2005) Deletion of Cg-emb in Corynebacterianeae leads to a novel truncated cell wall arabinogalactan, whereas inactivation of Cg-ubiA results in an arabinan-deficient mutant with a cell wall galactan core. J Biol Chem 280:32362–32371. https://doi.org/10.1074/jbc.M506339200
Alderwick LJ, Seidel M, Sahm H et al (2006) Identification of a novel arabinofuranosyltransferase (AftA) involved in cell wall arabinan biosynthesis in Mycobacterium tuberculosis. J Biol Chem 281:15653–15661. https://doi.org/10.1074/jbc.M600045200
Alderwick LJ, Dover LG, Veerapen N et al (2008) Expression, purification and characterisation of soluble GlfT and the identification of a novel galactofuranosyltransferase Rv3782 involved in priming GlfT-mediated galactan polymerisation in Mycobacterium tuberculosis. Protein Expr Purif 58:332–341. https://doi.org/10.1016/j.pep.2007.11.012
Alderwick LJ, Lloyd GS, Lloyd AJ et al (2011) Biochemical characterization of the Mycobacterium tuberculosis phosphoribosyl-1-pyrophosphate synthetase. Glycobiology 21:410–425. https://doi.org/10.1093/glycob/cwq173
Alderwick LJ, Birch HL, Krumbach K et al (2018) AftD functions as an alpha1→5 arabinofuranosyltransferase involved in the biosynthesis of the mycobacterial cell wall core. Cell Surf 1:2–14. https://doi.org/10.1016/j.tcsw.2017.10.001
Alibaud L, Pawelczyk J, Gannoun-Zaki L et al (2014) Increased phagocytosis of Mycobacterium marinum mutants defective in lipooligosaccharide production: a structure-activity relationship study. J Biol Chem 289:215–228. https://doi.org/10.1074/jbc.M113.525550
Alonso H, Parra J, Malaga W et al (2017) Protein O-mannosylation deficiency increases LprG-associated lipoarabinomannan release by Mycobacterium tuberculosis and enhances the TLR2-associated inflammatory response. Sci Rep 7:7913. https://doi.org/10.1038/s41598-017-08489-7
Alsteens D, Verbelen C, Dague E et al (2008) Organization of the mycobacterial cell wall: a nanoscale view. Pflugers Arch 456:117–125. https://doi.org/10.1007/s00424-007-0386-0
Angala SK, Belardinelli JM, Huc-Claustre E et al (2014) The cell envelope glycoconjugates of Mycobacterium tuberculosis. Crit Rev Biochem Mol Biol 49:361–399. https://doi.org/10.3109/10409238.2014.925420
Arbues A, Lugo-Villarino G, Neyrolles O et al (2014) Playing hide-and-seek with host macrophages through the use of mycobacterial cell envelope phthiocerol dimycocerosates and phenolic glycolipids. Front Cell Infect Microbiol 4:173. https://doi.org/10.3389/fcimb.2014.00173
Ariza MA, Martin-Luengo F, Valero-Guillen PL (1994) A family of diacyltrehaloses isolated from Mycobacterium fortuitum. Microbiology 140:1989–1994. https://doi.org/10.1099/13500872-140-8-1989
Asker MMS, Shawky BT (2010) Structural characterization and antioxidant activity of an extracellular polysaccharide isolated from Brevibacterium otitidis BTS 44. Food Chem 123:315–320. https://doi.org/10.1016/j.foodchem.2010.04.037
Ates LS, van der Woude AD, Bestebroer J et al (2016) The ESX-5 system of pathogenic mycobacteria is involved in capsule integrity and virulence through its substrate PPE10. PLoS Pathog 12:e1005696-26. https://doi.org/10.1371/journal.ppat.1005696
Azad AK, Sirakova TD, Rogers LM, Kolattukudy PE (1996) Targeted replacement of the mycocerosic acid synthase gene in Mycobacterium bovis BCG produces a mutant that lacks mycosides. Proc Natl Acad Sci USA 93:4787–4792
Azad AK, Sirakova TD, Fernandes ND, Kolattukudy PE (1997) Gene knockout reveals a novel gene cluster for the synthesis of a class of cell wall lipids unique to pathogenic mycobacteria. J Biol Chem 272:16741–16745
Backus KM, Dolan MA, Barry CS et al (2014) The three Mycobacterium tuberculosis antigen 85 isoforms have unique substrates and activities determined by non-active site regions. J Biol Chem 289:25041–25053. https://doi.org/10.1074/jbc.M114.581579
Ballou CE, Vilkas E, Lederer E (1963) Structural studies on the myo-inositol phospholipids of Mycobacterium tuberculosis (var. bovis, strain BCG). J Biol Chem 238:69–76
Bansal A, Kar D, Murugan RA et al (2015) A putative low-molecular-mass penicillin-binding protein (PBP) of Mycobacterium smegmatis exhibits prominent physiological characteristics of DD-carboxypeptidase and beta-lactamase. Microbiology 161:1081–1091. https://doi.org/10.1099/mic.0.000074
Bansal-Mutalik R, Nikaido H (2011) Quantitative lipid composition of cell envelopes of Corynebacterium glutamicum elucidated through reverse micelle extraction. Proc Natl Acad Sci USA 108:15360–15365. https://doi.org/10.1073/pnas.1112572108
Bansal-Mutalik R, Nikaido H (2014) Mycobacterial outer membrane is a lipid bilayer and the inner membrane is unusually rich in diacyl phosphatidylinositol dimannosides. Proc Natl Acad Sci USA 111:4958–4963. https://doi.org/10.1073/pnas.1403078111
Baranowski C, Welsh MA, Sham L-T, et al (2018) Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape. eLife. https://doi.org/10.7554/elife.37516
Barry CE, Lee RE, Mdluli K et al (1998) Mycolic acids: structure, biosynthesis and physiological functions. Prog Lipid Res 37:143–179
Batrakov SG, Bergelson LD (1978) Lipids of the streptomycetes structural investigation and biological interrelation: a review. Chem Phys Lipids 21:1–29
Baumgart M, Luder K, Grover S et al (2013) IpsA, a novel LacI-type regulator, is required for inositol-derived lipid formation in corynebacteria and mycobacteria. BMC Biol 11:122. https://doi.org/10.1186/1741-7007-11-122
Baumgart M, Schubert K, Bramkamp M, Frunzke J (2016) Impact of LytR-CpsA-Psr proteins on cell wall biosynthesis in Corynebacterium glutamicum. J Bacteriol 198:3045–3059. https://doi.org/10.1128/JB.00406-16
Belanger AE, Besra GS, Ford ME et al (1996) The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol. Proc Natl Acad Sci USA 93:11919–11924
Belanova M, Dianiskova P, Brennan PJ et al (2008) Galactosyl transferases in mycobacterial cell wall synthesis. J Bacteriol 190:1141–1145. https://doi.org/10.1128/JB.01326-07
Belardinelli JM, Larrouy-Maumus G, Jones V et al (2014) Biosynthesis and translocation of unsulfated acyltrehaloses in Mycobacterium tuberculosis. J Biol Chem 289:27952–27965. https://doi.org/10.1074/jbc.M114.581199
Belisle JT, Vissa VD, Sievert T et al (1997) Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis. Science 276:1420–1422
Bentley SD, Chater KF, Cerdeno-Tarraga A-M et al (2002) Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417:141–147. https://doi.org/10.1038/417141a
Bernut A, Viljoen A, Dupont C et al (2016) Insights into the smooth-to-rough transitioning in Mycobacterium bolletii unravels a functional Tyr residue conserved in all mycobacterial MmpL family members. Mol Microbiol 99:866–883. https://doi.org/10.1111/mmi.13283
Bertram R, Schlicht M, Mahr K et al (2004) In silico and transcriptional analysis of carbohydrate uptake systems of Streptomyces coelicolor A3(2). J Bacteriol 186:1362–1373. https://doi.org/10.1128/JB.186.5.1362-1373.2004
Bhamidi S, Scherman MS, Rithner CD et al (2008) The identification and location of succinyl residues and the characterization of the interior arabinan region allow for a model of the complete primary structure of Mycobacterium tuberculosis mycolyl arabinogalactan. J Biol Chem 283:12992–13000. https://doi.org/10.1074/jbc.M800222200
Bhamidi S, Scherman MS, Jones V et al (2011) Detailed structural and quantitative analysis reveals the spatial organization of the cell walls of in vivo grown Mycobacterium leprae and in vitro grown Mycobacterium tuberculosis. J Biol Chem 286:23168–23177. https://doi.org/10.1074/jbc.M110.210534
Bhatt K, Gurcha SS, Bhatt A et al (2007) Two polyketide-synthase-associated acyltransferases are required for sulfolipid biosynthesis in Mycobacterium tuberculosis. Microbiology 153:513–520. https://doi.org/10.1099/mic.0.2006/003103-0
Bhatt A, Brown AK, Singh A et al (2008) Loss of a mycobacterial gene encoding a reductase leads to an altered cell wall containing beta-oxo-mycolic acid analogs and accumulation of ketones. Chem Biol 15:930–939. https://doi.org/10.1016/j.chembiol.2008.07.007
Billman-Jacobe H, McConville MJ, Haites RE et al (1999) Identification of a peptide synthetase involved in the biosynthesis of glycopeptidolipids of Mycobacterium smegmatis. Mol Microbiol 33:1244–1253
Birch HL, Alderwick LJ, Bhatt A et al (2008) Biosynthesis of mycobacterial arabinogalactan: identification of a novel alpha(1→3) arabinofuranosyltransferase. Mol Microbiol 69:1191–1206. https://doi.org/10.1111/j.1365-2958.2008.06354.x
Birch HL, Alderwick LJ, Appelmelk BJ et al (2010) A truncated lipoglycan from mycobacteria with altered immunological properties. Proc Natl Acad Sci USA 107:2634–2639. https://doi.org/10.1073/pnas.0915082107
Biswas R, Dutta A, Dutta D et al (2015) Crystal structure of dehydratase component HadAB complex of mycobacterial FAS-II pathway. Biochem Biophys Res Commun 458:369–374. https://doi.org/10.1016/j.bbrc.2015.01.119
Bloch K (1977) Control mechanisms for fatty acid synthesis in Mycobacterium smegmatis. Adv Enzymol Relat Areas Mol Biol 45:1–84
Bou Raad R, Meniche X, de Sousa-d’Auria C et al (2010) A deficiency in arabinogalactan biosynthesis affects Corynebacterium glutamicum mycolate outer membrane stability. J Bacteriol 192:2691–2700. https://doi.org/10.1128/JB.00009-10
Boutte CC, Baer CE, Papavinasasundaram K, et al (2016) A cytoplasmic peptidoglycan amidase homologue controls mycobacterial cell wall synthesis. eLife 5:a021113. https://doi.org/10.7554/elife.14590
Brammer Basta LA, Ghosh A, Pan Y et al (2015) Loss of a functionally and structurally distinct LD-transpeptidase, LdtMt5, compromises cell wall integrity in Mycobacterium tuberculosis. J Biol Chem 290:25670–25685. https://doi.org/10.1074/jbc.M115.660753
Brennan PJ, Lehane DP (1971) The phospholipids of corynebacteria. Lipids 6:401–409
Brindley DN, Matsumura S, Bloch K (1969) Mycobacterium phlei fatty acid synthetase—a bacterial multienzyme complex. Nature 224:666–669. https://doi.org/10.1038/224666a0
Burguiere A, Hitchen PG, Dover LG et al (2005) LosA, a key glycosyltransferase involved in the biosynthesis of a novel family of glycosylated acyltrehalose lipooligosaccharides from Mycobacterium marinum. J Biol Chem 280:42124–42133. https://doi.org/10.1074/jbc.M507500200
Camacho LR, Ensergueix D, Perez E et al (1999) Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol Microbiol 34:257–267
Camacho LR, Constant P, Raynaud C et al (2001) Analysis of the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Evidence that this lipid is involved in the cell wall permeability barrier. J Biol Chem 276:19845–19854. https://doi.org/10.1074/jbc.M100662200
Cambier CJ, Takaki KK, Larson RP et al (2014) Mycobacteria manipulate macrophage recruitment through coordinated use of membrane lipids. Nature 505:218–222. https://doi.org/10.1038/nature12799
Cambier CJ, O’Leary SM, O’Sullivan MP et al (2017) Phenolic glycolipid facilitates mycobacterial escape from microbicidal tissue-resident macrophages. Immunity 47:552–565.e4. https://doi.org/10.1016/j.immuni.2017.08.003
Cashmore TJ, Klatt S, Yamaryo-Botte Y et al (2017) Identification of a membrane protein required for lipomannan maturation and lipoarabinomannan synthesis in Corynebacterineae. J Biol Chem 292:4976–4986. https://doi.org/10.1074/jbc.M116.772202
Castro-Bravo N, Wells JM, Margolles A, Ruas-Madiedo P (2018) Interactions of surface exopolysaccharides from Bifidobacterium and Lactobacillus within the intestinal environment. Front Microbiol 9:2426. https://doi.org/10.3389/fmicb.2018.02426
Celler K, Koning RI, Willemse J et al (2016) Cross-membranes orchestrate compartmentalization and morphogenesis in Streptomyces. Nat Commun 7:1–8. https://doi.org/10.1038/ncomms11836
Chami M, Bayan N, Peyret JL et al (1997) The S-layer protein of Corynebacterium glutamicum is anchored to the cell wall by its C-terminal hydrophobic domain. Mol Microbiol 23:483–492
Chao MC, Kieser KJ, Minami S et al (2013) Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria. PLoS Pathog 9:e1003197. https://doi.org/10.1371/journal.ppat.1003197.s011
Chapman GB, Hanks JH, Wallace JH (1959) An electron microscope study of the disposition and fine structure of Mycobacterium lepraemurium in mouse spleen. J Bacteriol 77:205–211
Chatterjee D, Khoo KH (2001) The surface glycopeptidolipids of mycobacteria: structures and biological properties. Cell Mol Life Sci 58:2018–2042. https://doi.org/10.1007/PL00000834
Chaudhary DK, Kim J (2018) Rhodococcus olei sp. nov., with the ability to degrade petroleum oil, isolated from oil-contaminated soil. Int J Syst Evol Microbiol 68:1749–1756. https://doi.org/10.1099/ijsem.0.002750
Chauhan A, Lofton H, Maloney E et al (2006) Interference of Mycobacterium tuberculosis cell division by Rv2719c, a cell wall hydrolase. Mol Microbiol 62:132–147. https://doi.org/10.1111/j.1365-2958.2006.05333.x
Chavadi SS, Edupuganti UR, Vergnolle O et al (2011) Inactivation of tesA reduces cell wall lipid production and increases drug susceptibility in mycobacteria. J Biol Chem 286:24616–24625. https://doi.org/10.1074/jbc.M111.247601
Chen Y-Y, Yang F-L, Wu S-H et al (2015) Mycobacterium marinum mmar_2318 and mmar_2319 are responsible for lipooligosaccharide biosynthesis and virulence toward Dictyostelium. Front Microbiol 6:1458. https://doi.org/10.3389/fmicb.2015.01458
Choudhuri BS, Bhakta S, Barik R et al (2002) Overexpression and functional characterization of an ABC (ATP-binding cassette) transporter encoded by the genes drrA and drrB of Mycobacterium tuberculosis. Biochem J 367:279–285. https://doi.org/10.1042/BJ20020615
Christova N, Lang S, Wray V et al (2015) Production, structural elucidation, and in vitro antitumor activity of trehalose lipid biosurfactant from Nocardia farcinica strain. J Microbiol Biotechnol 25:439–447. https://doi.org/10.4014/jmb.1406.06025
Collins MD, Goodfellow M, Minnikin DE (1982) Fatty acid composition of some mycolic acid-containing coryneform bacteria. J Gen Microbiol 128:2503–2509. https://doi.org/10.1099/00221287-128-11-2503
Converse SE, Mougous JD, Leavell MD et al (2003) MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence. Proc Natl Acad Sci USA 100:6121–6126. https://doi.org/10.1073/pnas.1030024100
Cot M, Ray A, Gilleron M et al (2011) Lipoteichoic acid in Streptomyces hygroscopicus: structural model and immunomodulatory activities. PLoS ONE 6:e26316. https://doi.org/10.1371/journal.pone.0026316
Cox JS, Chen B, McNeil M, Jacobs WR (1999) Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature 402:79–83. https://doi.org/10.1038/47042
Crellin PK, Kovacevic S, Martin KL et al (2008) Mutations in pimE restore lipoarabinomannan synthesis and growth in a Mycobacterium smegmatis lpqW mutant. J Bacteriol 190:3690–3699. https://doi.org/10.1128/JB.00200-08
Crellin PK, Luo C-Y, Morita YS (2013) Metabolism of plasma membrane lipids in mycobacteria and corynebacteria. In: Baez RV (ed) Lipid Metabolism. InTech, London, UK, pp 119–148
Cywes C, Hoppe HC, Daffe M, Ehlers MR (1997) Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent. Infect Immun 65:4258–4266
Daffe M, Draper P (1998) The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol 39:131–203
Daffe M, Etienne G (1999) The capsule of Mycobacterium tuberculosis and its implications for pathogenicity. Tuber Lung Dis 79:153–169
Daffe M, Laneelle MA (1988) Distribution of phthiocerol diester, phenolic mycosides and related compounds in mycobacteria. J Gen Microbiol 134:2049–2055. https://doi.org/10.1099/00221287-134-7-2049
Daffe M, Brennan PJ, McNeil M (1990) Predominant structural features of the cell wall arabinogalactan of Mycobacterium tuberculosis as revealed through characterization of oligoglycosyl alditol fragments by gas chromatography/mass spectrometry and by 1H and 13C NMR analyses. J Biol Chem 265:6734–6743
Daffe M, McNeil M, Brennan PJ (1991) Novel type-specific lipooligosaccharides from Mycobacterium tuberculosis. Biochemistry 30:378–388
Daffe M, McNeil M, Brennan PJ (1993) Major structural features of the cell wall arabinogalactans of Mycobacterium, Rhodococcus, and Nocardia spp. Carbohydr Res 249:383–398
Daffe M, Crick DC, Jackson M (2014) Genetics of capsular polysaccharides and cell envelope (glyco)lipids. Microbiol Spectr 2:MGM2-0021-2013. https://doi.org/10.1128/microbiolspec.mgm2-0021-2013
Daniel RA, Errington J (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113:767–776. https://doi.org/10.1016/S0092-8674(03)00421-5
Dhiman RK, Dinadayala P, Ryan GJ et al (2011) Lipoarabinomannan localization and abundance during growth of Mycobacterium smegmatis. J Bacteriol 193:5802–5809. https://doi.org/10.1128/JB.05299-11
Dianiskova P, Kordulakova J, Skovierova H et al (2011) Investigation of ABC transporter from mycobacterial arabinogalactan biosynthetic cluster. Gen Physiol Biophys 30:239–250. https://doi.org/10.4149/gpb_2011_03_239
Domenech P, Reed MB, Dowd CS et al (2004) The role of MmpL8 in sulfatide biogenesis and virulence of Mycobacterium tuberculosis. J Biol Chem 279:21257–21265. https://doi.org/10.1074/jbc.M400324200
Donovan C, Bramkamp M (2014) Cell division in Corynebacterineae. Front Microbiol 5:132. https://doi.org/10.3389/fmicb.2014.00132
Donovan C, Sieger B, Krämer R, Bramkamp M (2012) A synthetic Escherichia coli system identifies a conserved origin tethering factor in Actinobacteria. Mol Microbiol 84:105–116. https://doi.org/10.1111/j.1365-2958.2012.08011.x
Drage MG, Tsai H-C, Pecora ND et al (2010) Mycobacterium tuberculosis lipoprotein LprG (Rv1411c) binds triacylated glycolipid agonists of Toll-like receptor 2. Nat Struct Mol Biol 17:1088–1095. https://doi.org/10.1038/nsmb.1869
Draper P, Kandler O, Darbre A (1987) Peptidoglycan and arabinogalactan of Mycobacterium leprae. J Gen Microbiol 133:1187–1194. https://doi.org/10.1099/00221287-133-5-1187
Draper P, Khoo KH, Chatterjee D et al (1997) Galactosamine in walls of slow-growing mycobacteria. Biochem J 327(Pt 2):519–525
Duan X, Xiang X, Xie J (2014) Crucial components of mycobacterium type II fatty acid biosynthesis (Fas-II) and their inhibitors. FEMS Microbiol Lett 360:87–99. https://doi.org/10.1111/1574-6968.12597
Dubey VS, Sirakova TD, Kolattukudy PE (2002) Disruption of msl3 abolishes the synthesis of mycolipanoic and mycolipenic acids required for polyacyltrehalose synthesis in Mycobacterium tuberculosis H37Rv and causes cell aggregation. Mol Microbiol 45:1451–1459
Dubey VS, Sirakova TD, Cynamon MH, Kolattukudy PE (2003) Biochemical function of msl5 (pks8 plus pks17) in Mycobacterium tuberculosis H37Rv: biosynthesis of monomethyl branched unsaturated fatty acids. J Bacteriol 185:4620–4625. https://doi.org/10.1128/JB.185.15.4620-4625.2003
Dubois V, Viljoen A, Laencina L et al (2018) MmpL8MAB controls Mycobacterium abscessus virulence and production of a previously unknown glycolipid family. Proc Natl Acad Sci USA 115:E10147–E10156. https://doi.org/10.1073/pnas.1812984115
Eagen WJ, Baumoel LR, Osman SH, et al (2018) Deletion of PimE mannosyltransferase results in increased copper sensitivity in Mycobacterium smegmatis. FEMS Microbiol Lett 365:fny025. https://doi.org/10.1093/femsle/fny025
Ealand C, Rimal B, Chang J et al (2018) Resuscitation-promoting factors are required for Mycobacterium smegmatis biofilm formation. Appl Environ Microbiol 84:643. https://doi.org/10.1128/AEM.00687-18
Eckstein TM, Silbaq FS, Chatterjee D et al (1998) Identification and recombinant expression of a Mycobacterium avium rhamnosyltransferase gene (rtfA) involved in glycopeptidolipid biosynthesis. J Bacteriol 180:5567–5573
Escuyer VE, Lety MA, Torrelles JB et al (2001) The role of the embA and embB gene products in the biosynthesis of the terminal hexaarabinofuranosyl motif of Mycobacterium smegmatis arabinogalactan. J Biol Chem 276:48854–48862. https://doi.org/10.1074/jbc.M102272200
Espuny MJ, Egjido S, Mercade ME, Manresa A (1995) Characterization of trehalose tetraester produced by a waste lube oil degrader Rhodococcus sp. 51T7. Toxicol Environ Chem 48:83–88. https://doi.org/10.1080/02772249509358154
Etienne G, Malaga W, Laval F et al (2009) Identification of the polyketide synthase involved in the biosynthesis of the surface-exposed lipooligosaccharides in mycobacteria. J Bacteriol 191:2613–2621. https://doi.org/10.1128/JB.01235-08
Ferreras JA, Stirrett KL, Lu X et al (2008) Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism and small-molecule inhibition of polyketide chain initiation. Chem Biol 15:51–61. https://doi.org/10.1016/j.chembiol.2007.11.010
Fitzmaurice AM, Kolattukudy PE (1997) Open reading frame 3, which is adjacent to the mycocerosic acid synthase gene, is expressed as an acyl coenzyme A synthase in Mycobacterium bovis BCG. J Bacteriol 179:2608–2615
Fitzmaurice AM, Kolattukudy PE (1998) An acyl-CoA synthase (acoas) gene adjacent to the mycocerosic acid synthase (mas) locus is necessary for mycocerosyl lipid synthesis in Mycobacterium tuberculosis var. bovis BCG. J Biol Chem 273:8033–8039
Fiuza M, Canova MJ, Patin D et al (2008) The MurC ligase essential for peptidoglycan biosynthesis is regulated by the serine/threonine protein kinase PknA in Corynebacterium glutamicum. J Biol Chem 283:36553–36563. https://doi.org/10.1074/jbc.M807175200
Flärdh K (2003) Essential role of DivIVA in polar growth and morphogenesis in Streptomyces coelicolor A3(2). Mol Microbiol 49:1523–1536
Flärdh K, Richards DM, Hempel AM et al (2012) Regulation of apical growth and hyphal branching in Streptomyces. Curr Opin Microbiol 15:737–743. https://doi.org/10.1016/j.mib.2012.10.012
Frehel C, Ryter A, Rastogi N, David H (1986) The electron-transparent zone in phagocytized Mycobacterium avium and other mycobacteria: formation, persistence and role in bacterial survival. Ann Inst Pasteur Microbiol 137B:239–257
Fujiwara N, Nakata N, Maeda S et al (2007) Structural characterization of a specific glycopeptidolipid containing a novel N-acyl-deoxy sugar from Mycobacterium intracellulare serotype 7 and genetic analysis of its glycosylation pathway. J Bacteriol 189:1099–1108. https://doi.org/10.1128/JB.01471-06
Fukuda T, Matsumura T, Ato M, et al (2013) Critical roles for lipomannan and lipoarabinomannan in cell wall integrity of mycobacteria and pathogenesis of tuberculosis. mBio 4:e00472–12. https://doi.org/10.1128/mbio.00472-12
Gao B, Gupta RS (2012) Phylogenetic framework and molecular signatures for the main clades of the phylum Actinobacteria. Microbiol Mol Biol Rev 76:66–112. https://doi.org/10.1128/MMBR.05011-11
Garcia-Heredia A, Pohane AA, Melzer ES, et al (2018) Peptidoglycan precursor synthesis along the sidewall of pole-growing mycobacteria. eLife 7:100. https://doi.org/10.7554/elife.37243
Gavalda S, Leger M, Van-der-Rest B et al (2009) The Pks13/FadD32 crosstalk for the biosynthesis of mycolic acids in Mycobacterium tuberculosis. J Biol Chem 284:19255–19264. https://doi.org/10.1074/jbc.M109.006940
Gavalda S, Bardou F, Laval F et al (2014) The polyketide synthase Pks13 catalyzes a novel mechanism of lipid transfer in mycobacteria. Chem Biol 21:1660–1669. https://doi.org/10.1016/j.chembiol.2014.10.011
Geurtsen J, Chedammi S, Mesters J et al (2009) Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: involvement of mycobacterial capsular polysaccharides in host immune modulation. J Immunol 183:5221–5231. https://doi.org/10.4049/jimmunol.0900768
Gibson KJC, Eggeling L, Maughan WN et al (2003) Disruption of Cg-Ppm1, a polyprenyl monophosphomannose synthase, and the generation of lipoglycan-less mutants in Corynebacterium glutamicum. J Biol Chem 278:40842–40850. https://doi.org/10.1074/jbc.M307988200
Gibson KJC, Gilleron M, Constant P et al (2005) A lipomannan variant with strong TLR-2-dependent pro-inflammatory activity in Saccharothrix aerocolonigenes. J Biol Chem 280:28347–28356. https://doi.org/10.1074/jbc.M505498200
Gilby AR, Few AV, McQuillen K (1958) The chemical composition of the protoplast membrane of Micrococcus lysodeikticus. Biochim Biophys Acta 29:21–29
Gilleron M, Vercauteren J, Puzo G (1993) Lipooligosaccharidic antigen containing a novel C4-branched 3,6-dideoxy-alpha-hexopyranose typifies Mycobacterium gastri. J Biol Chem 268:3168–3179
Gilleron M, Garton NJ, Nigou J et al (2005) Characterization of a truncated lipoarabinomannan from the Actinomycete Turicella otitidis. J Bacteriol 187:854–861. https://doi.org/10.1128/JB.187.3.854-861.2005
Gokhale RS, Saxena P, Chopra T, Mohanty D (2007) Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat Prod Rep 24:267–277. https://doi.org/10.1039/b616817p
Goodfellow M, Weaver CR, Minnikin DE (1982) Numerical classification of some rhodococci, corynebacteria and related organisms. J Gen Microbiol 128:731–745. https://doi.org/10.1099/00221287-128-4-731
Goren MB (1970) Sulfolipid I of Mycobacterium tuberculosis, strain H37Rv. II. Structural studies. Biochim Biophys Acta 210:127–138
Goren MB, Brokl O, Schaefer WB (1974) Lipids of putative relevance to virulence in Mycobacterium tuberculosis: phthiocerol dimycocerosate and the attenuation indicator lipid. Infect Immun 9:150–158
Goude R, Amin AG, Chatterjee D, Parish T (2008) The critical role of embC in Mycobacterium tuberculosis. J Bacteriol 190:4335–4341. https://doi.org/10.1128/JB.01825-07
Grover S, Alderwick LJ, Mishra AK et al (2014) Benzothiazinones mediate killing of Corynebacterineae by blocking decaprenyl phosphate recycling involved in cell wall biosynthesis. J Biol Chem 289:6177–6187. https://doi.org/10.1074/jbc.M113.522623
Grzegorzewicz AE, Pham H, Gundi VAKB, et al (2012) Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane. Nat Chem Biol 1–8. https://doi.org/10.1038/nchembio.794
Grzegorzewicz AE, de Sousa-d’Auria C, McNeil MR et al (2016) Assembling of the Mycobacterium tuberculosis cell wall core. J Biol Chem 291:18867–18879. https://doi.org/10.1074/jbc.M116.739227
Guerin ME, Kaur D, Somashekar BS et al (2009) New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB’ is an essential enzyme of Mycobacterium smegmatis. J Biol Chem 284:25687–25696. https://doi.org/10.1074/jbc.M109.030593
Gupta R, Lavollay M, Mainardi J-L et al (2010) The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat Med 16:466–469. https://doi.org/10.1038/nm.2120
Gurcha SS, Baulard AR, Kremer L et al (2002) Ppm1, a novel polyprenol monophosphomannose synthase from Mycobacterium tuberculosis. Biochem J 365:441–450
Gutierrez AV, Viljoen A, Ghigo E et al (2018) Glycopeptidolipids, a double-edged sword of the Mycobacterium abscessus complex. Front Microbiol 9:1145. https://doi.org/10.3389/fmicb.2018.01145
Haites RE, Morita YS, McConville MJ, Billman-Jacobe H (2005) Function of phosphatidylinositol in mycobacteria. J Biol Chem 280:10981–10987. https://doi.org/10.1074/jbc.M413443200
Hamada M, Iino T, Tamura T et al (2009) Serinibacter salmoneus gen. nov., sp. nov., an actinobacterium isolated from the intestinal tract of a fish, and emended descriptions of the families Beutenbergiaceae and Bogoriellaceae. Int J Syst Evol Microbiol 59:2809–2814. https://doi.org/10.1099/ijs.0.011106-0
Hansmeier N, Albersmeier A, Tauch A et al (2006) The surface (S)-layer gene cspB of Corynebacterium glutamicum is transcriptionally activated by a LuxR-type regulator and located on a 6 kb genomic island absent from the type strain ATCC 13032. Microbiology 152:923–935. https://doi.org/10.1099/mic.0.28673-0
Harrison J, Lloyd G, Joe M, et al (2016) Lcp1 is a phosphotransferase responsible for ligating arabinogalactan to peptidoglycan in Mycobacterium tuberculosis. mBio. https://doi.org/10.1128/mbio.00972-16
Hatzios SK, Schelle MW, Holsclaw CM et al (2009) PapA3 is an acyltransferase required for polyacyltrehalose biosynthesis in Mycobacterium tuberculosis. J Biol Chem 284:12745–12751. https://doi.org/10.1074/jbc.M809088200
Hayashi JM, Luo C-Y, Mayfield JA et al (2016) Spatially distinct and metabolically active membrane domain in mycobacteria. Proc Natl Acad Sci USA 113:5400–5405. https://doi.org/10.1073/pnas.1525165113
Hayashi JM, Richardson K, Melzer ES, et al (2018) Stress-induced reorganization of the mycobacterial membrane domain. mBio 9:e01823–17. https://doi.org/10.1128/mbio.01823-17
Hempel AM, Wang S-B, Letek M et al (2008) Assemblies of DivIVA mark sites for hyphal branching and can establish new zones of cell wall growth in Streptomyces coelicolor. J Bacteriol 190:7579–7583. https://doi.org/10.1128/JB.00839-08
Hett EC, Chao MC, Steyn AJ et al (2007) A partner for the resuscitation-promoting factors of Mycobacterium tuberculosis. Mol Microbiol 66:658–668. https://doi.org/10.1111/j.1365-2958.2007.05945.x
Hett EC, Chao MC, Deng LL, Rubin EJ (2008) A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor. PLoS Pathog 4:e1000001. https://doi.org/10.1371/journal.ppat.1000001
Hett EC, Chao MC, Rubin EJ (2010) Interaction and modulation of two antagonistic cell wall enzymes of mycobacteria. PLoS Pathog 6:e1001020. https://doi.org/10.1371/journal.ppat.1001020.s002
Hidalgo-Cantabrana C, Sanchez B, Milani C et al (2014) Genomic overview and biological functions of exopolysaccharide biosynthesis in Bifidobacterium spp. Appl Environ Microbiol 80:9–18. https://doi.org/10.1128/AEM.02977-13
Hodgson DA (2000) Primary metabolism and its control in streptomycetes: a most unusual group of bacteria. Adv Microb Physiol 42:47–238
Hoffmann C, Leis A, Niederweis M et al (2008) Disclosure of the mycobacterial outer membrane: cryo-electron tomography and vitreous sections reveal the lipid bilayer structure. Proc Natl Acad Sci USA 105:3963–3967. https://doi.org/10.1073/pnas.0709530105
Hoischen C, Gura K, Luge C, Gumpert J (1997) Lipid and fatty acid composition of cytoplasmic membranes from Streptomyces hygroscopicus and its stable protoplast-type L form. J Bacteriol 179:3430–3436
Hong S, Cheng T-Y, Layre E et al (2012) Ultralong C100 mycolic acids support the assignment of Segniliparus as a new bacterial genus. PLoS ONE 7:e39017. https://doi.org/10.1371/journal.pone.0039017
Howlett R, Anttonen K, Read N, Smith MCM (2018) Disruption of the GDP-mannose synthesis pathway in Streptomyces coelicolor results in antibiotic hyper-susceptible phenotypes. Microbiology 164:614–624. https://doi.org/10.1099/mic.0.000636
Hunter SW, Murphy RC, Clay K et al (1983) Trehalose-containing lipooligosaccharides. A new class of species-specific antigens from Mycobacterium. J Biol Chem 258:10481–10487
Hunter SW, Fujiwara T, Murphy RC, Brennan PJ (1984) N-acylkansosamine. A novel N-acylamino sugar from the trehalose-containing lipooligosaccharide antigens of Mycobacterium kansasii. J Biol Chem 259:9729–9734
Hunter SW, Gaylord H, Brennan PJ (1986) Structure and antigenicity of the phosphorylated lipopolysaccharide antigens from the leprosy and tubercle bacilli. J Biol Chem 261:12345–12351
Ishikawa E, Mori D, Yamasaki S (2017) Recognition of mycobacterial lipids by immune receptors. Trends Immunol 38:66–76. https://doi.org/10.1016/j.it.2016.10.009
Jackson M, Crick DC, Brennan PJ (2000) Phosphatidylinositol is an essential phospholipid of mycobacteria. J Biol Chem 275:30092–30099. https://doi.org/10.1074/jbc.M004658200
Jain M, Cox JS (2005) Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis. PLoS Pathog 1:e2. https://doi.org/10.1371/journal.ppat.0010002
Jamet S, Slama N, Domingues J et al (2015) The non-essential mycolic acid biosynthesis genes hadA and hadC contribute to the physiology and fitness of Mycobacterium smegmatis. PLoS ONE 10:e0145883. https://doi.org/10.1371/journal.pone.0145883
Jankute M, Cox JAG, Harrison J, Besra GS (2015) Assembly of the mycobacterial cell wall. Annu Rev Microbiol 69:405–423. https://doi.org/10.1146/annurev-micro-091014-104121
Jankute M, Alderwick LJ, Noack S et al (2017) Disruption of mycobacterial AftB results in complete loss of terminal β(1→2) arabinofuranose residues of lipoarabinomannan. ACS Chem Biol 12:183–190. https://doi.org/10.1021/acschembio.6b00898
Jankute M, Alderwick LJ, Moorey AR et al (2018) The singular Corynebacterium glutamicum Emb arabinofuranosyltransferase polymerises the alpha(1→5) arabinan backbone in the early stages of cell wall arabinan biosynthesis. Cell Surf 2:38–53. https://doi.org/10.1016/j.tcsw.2018.06.003
Jeevarajah D, Patterson JH, McConville MJ, Billman-Jacobe H (2002) Modification of glycopeptidolipids by an O-methyltransferase of Mycobacterium smegmatis. Microbiology 148:3079–3087. https://doi.org/10.1099/00221287-148-10-3079
Jeevarajah D, Patterson JH, Taig E et al (2004) Methylation of GPLs in Mycobacterium smegmatis and Mycobacterium avium. J Bacteriol 186:6792–6799. https://doi.org/10.1128/JB.186.20.6792-6799.2004
Jiang T, He L, Zhan Y, et al (2011) The effect of MSMEG_6402 gene disruption on the cell wall structure of Mycobacterium smegmatis. Microb Pathog 1–5. https://doi.org/10.1016/j.micpath.2011.04.005
Jin Y, Xin Y, Zhang W, Ma Y (2010) Mycobacterium tuberculosis Rv1302 and Mycobacterium smegmatis MSMEG_4947 have WecA function and MSMEG_4947 is required for the growth of M. smegmatis. FEMS Microbiol Lett 310:54–61. https://doi.org/10.1111/j.1574-6968.2010.02045.x
Jyothikumar V, Klanbut K, Tiong J et al (2012) Cardiolipin synthase is required for Streptomyces coelicolor morphogenesis. Mol Microbiol 84:181–197. https://doi.org/10.1111/j.1365-2958.2012.08018.x
Kallenius G, Correia-Neves M, Buteme H et al (2016) Lipoarabinomannan, and its related glycolipids, induce divergent and opposing immune responses to Mycobacterium tuberculosis depending on structural diversity and experimental variations. Tuberculosis 96:120–130. https://doi.org/10.1016/j.tube.2015.09.005
Kang CM, Nyayapathy S, Lee JY et al (2008) Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria. Microbiology 154:725–735. https://doi.org/10.1099/mic.0.2007/014076-0
Kato K, Strominger JL, Kotani S (1968) Structure of the cell wall of Corynebacterium diphtheriae. I. Mechanism of hydrolysis by the L-3 enzyme and the structure of the peptide. Biochemistry 7:2762–2773
Kaur D, Berg S, Dinadayala P et al (2006) Biosynthesis of mycobacterial lipoarabinomannan: role of a branching mannosyltransferase. Proc Natl Acad Sci USA 103:13664–13669. https://doi.org/10.1073/pnas.0603049103
Kaur D, McNeil MR, Khoo K-H et al (2007) New insights into the biosynthesis of mycobacterial lipomannan arising from deletion of a conserved gene. J Biol Chem 282:27133–27140. https://doi.org/10.1074/jbc.M703389200
Kaur D, Obregon-Henao A, Pham H et al (2008) Lipoarabinomannan of Mycobacterium: mannose capping by a multifunctional terminal mannosyltransferase. Proc Natl Acad Sci USA 105:17973–17977. https://doi.org/10.1073/pnas.0807761105
Kaur D, Angala SK, Wu SW et al (2014) A single arabinan chain is attached to the phosphatidylinositol mannosyl core of the major immunomodulatory mycobacterial cell envelope glycoconjugate, lipoarabinomannan. J Biol Chem 289:30249–30256. https://doi.org/10.1074/jbc.M114.599415
Kawanami J, Kimura A, Otsuka H (1968) Siolipin A: a new lipoamino acid ester isolated from Streptomyces sioyaensis. Biochim Biophys Acta 152:808–810
Kieser KJ, Baranowski C, Chao MC et al (2015a) Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility. Proc Natl Acad Sci USA 112:13087–13092. https://doi.org/10.1073/pnas.1514135112
Kieser KJ, Boutte CC, Kester JC et al (2015b) Phosphorylation of the peptidoglycan synthase PonA1 governs the rate of polar elongation in mycobacteria. PLoS Pathog 11:e1005010. https://doi.org/10.1371/journal.ppat.1005010
Kimura A, Kawanami J, Otsuka H (1967) Lipids of Streptomyces sioyaensis. J Biochem 62:384–385
Klatt S, Brammananth R, O’Callaghan S et al (2018) Identification of novel lipid modifications and intermembrane dynamics in Corynebacterium glutamicum using high-resolution mass spectrometry. J Lipid Res 59:1190–1204. https://doi.org/10.1194/jlr.M082784
Koch D, Schleifer KH, Kandler O (1970) The amino acid sequence of the serine and aspartic acid containing mureins of Bifidobacterium bifidum Orla Jensen. Z Naturforsch B 25:1294–1301
Kochetkov NK, Sviridov AF, Arifkhodzhaev KA et al (1979) The structure of the extracellular polysaccharide from Mycobacterium lacticolum strain 121. Carbohydr Res 71:193–203. https://doi.org/10.1016/S0008-6215(00)86070-X
Kondo T, Yamamoto D, Yokota A et al (2000) Gordonan, an acidic polysaccharide with cell aggregation-inducing activity in insect BM-N4 cells, produced by Gordonia sp. Biosci Biotechnol Biochem 64:2388–2394. https://doi.org/10.1271/bbb.64.2388
Kordulakova J, Gilleron M, Mikusova K et al (2002) Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria. J Biol Chem 277:31335–31344. https://doi.org/10.1074/jbc.M204060200
Kordulakova J, Gilleron M, Puzo G et al (2003) Identification of the required acyltransferase step in the biosynthesis of the phosphatidylinositol mannosides of Mycobacterium species. J Biol Chem 278:36285–36295. https://doi.org/10.1074/jbc.M303639200
Koronelli TV (1988) Investigation of the lipids of saprophytic mycobacteria in the U.S.S.R. J Chromatogr 440:479–486
Koster S, Upadhyay S, Chandra P et al (2017) Mycobacterium tuberculosis is protected from NADPH oxidase and LC3-associated phagocytosis by the LCP protein CpsA. Proc Natl Acad Sci USA 114:E8711–E8720. https://doi.org/10.1073/pnas.1707792114
Kovacevic S, Anderson D, Morita YS et al (2006) Identification of a novel protein with a role in lipoarabinomannan biosynthesis in mycobacteria. J Biol Chem 281:9011–9017. https://doi.org/10.1074/jbc.M511709200
Kozikowski AP, Onajole OK, Stec J et al (2017) Targeting mycolic acid transport by indole-2-carboxamides for the treatment of Mycobacterium abscessus infections. J Med Chem 60:5876–5888. https://doi.org/10.1021/acs.jmedchem.7b00582
Kugler JH, Muhle-Goll C, Kuhl B et al (2014) Trehalose lipid biosurfactants produced by the actinomycetes Tsukamurella spumae and T. pseudospumae. Appl Microbiol Biotechnol 98:8905–8915. https://doi.org/10.1007/s00253-014-5972-4
Kumar P, Schelle MW, Jain M et al (2007) PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Proc Natl Acad Sci USA 104:11221–11226. https://doi.org/10.1073/pnas.0611649104
Kumar P, Arora K, Lloyd JR et al (2012) Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis. Mol Microbiol 86:367–381. https://doi.org/10.1111/j.1365-2958.2012.08199.x
Laneelle MA, Prome D, Laneelle G, Prome JC (1990) Ornithine lipid of Mycobacterium tuberculosis: its distribution in some slow- and fast-growing mycobacteria. J Gen Microbiol 136:773–778. https://doi.org/10.1099/00221287-136-4-773
Laneelle M-A, Launay A, Spina L et al (2012) A novel mycolic acid species defines two novel genera of the Actinobacteria, Hoyosella and Amycolicicoccus. Microbiology 158:843–855. https://doi.org/10.1099/mic.0.055509-0
Laneelle M-A, Eynard N, Spina L et al (2013) Structural elucidation and genomic scrutiny of the C60–C100 mycolic acids of Segniliparus rotundus. Microbiology 159:191–203. https://doi.org/10.1099/mic.0.063479-0
Lang S, Philp JC (1998) Surface-active lipids in rhodococci. Antonie Van Leeuwenhoek 74:59–70
Larrouy-Maumus G, Skovierova H, Dhouib R et al (2012) A small multidrug resistance-like transporter involved in the arabinosylation of arabinogalactan and lipoarabinomannan in mycobacteria. J Biol Chem 287:39933–39941. https://doi.org/10.1074/jbc.M112.400986
Lavollay M, Arthur M, Fourgeaud M et al (2008) The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation. J Bacteriol 190:4360–4366. https://doi.org/10.1128/JB.00239-08
Lavollay M, Arthur M, Fourgeaud M et al (2009) The beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium. Mol Microbiol 74:650–661. https://doi.org/10.1111/j.1365-2958.2009.06887.x
Lavollay M, Fourgeaud M, Herrmann J-L et al (2011) The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidases. J Bacteriol 193:778–782. https://doi.org/10.1128/JB.00606-10
Lea-Smith DJ, Pyke JS, Tull D et al (2007) The reductase that catalyzes mycolic motif synthesis is required for efficient attachment of mycolic acids to arabinogalactan. J Biol Chem 282:11000–11008. https://doi.org/10.1074/jbc.M608686200
Lea-Smith DJ, Martin KL, Pyke JS et al (2008) Analysis of a new mannosyltransferase required for the synthesis of phosphatidylinositol mannosides and lipoarabinomannan reveals two lipomannan pools in Corynebacterineae. J Biol Chem 283:6773–6782. https://doi.org/10.1074/jbc.M707139200
Lechevalier MP, De Bievre C, Lechevalier H (1977) Chemotaxonomy of aerobic Actinomycetes: phospholipid composition. Biochem Syst Ecol 5:249–260. https://doi.org/10.1016/0305-1978(77)90021-7
Lee YC, Ballou CE (1964) Structural studies on the myo-inositol mannosides from the glycolipids of Mycobacterium tuberculosis and Mycobacterium phlei. J Biol Chem 239:1316–1327
Lee RE, Mikusova K, Brennan PJ, Besra GS (1995) Synthesis of the arabinose donor beta-d-arabinofuranosyl-1-monophosphoryldecaprenol, development of a basic arabinosyl-transferase assay, and identification of ethambutol as an arabinosyl transferase inhibitor. J Am Chem Soc 117:11829–11832. https://doi.org/10.1021/ja00153a002
Lee RE, Brennan PJ, Besra GS (1997) Mycobacterial arabinan biosynthesis: the use of synthetic arabinoside acceptors in the development of an arabinosyl transfer assay. Glycobiology 7:1121–1128
Lee A, Wu S-W, Scherman MS et al (2006) Sequencing of oligoarabinosyl units released from mycobacterial arabinogalactan by endogenous arabinanase: identification of distinctive and novel structural motifs. Biochemistry 45:15817–15828. https://doi.org/10.1021/bi060688d
Lee JS, Krause R, Schreiber J et al (2008) Mutation in the transcriptional regulator PhoP contributes to avirulence of Mycobacterium tuberculosis H37Ra strain. Cell Host Microbe 3:97–103. https://doi.org/10.1016/j.chom.2008.01.002
Lefebvre C, Boulon R, Ducoux M et al (2018) HadD, a novel fatty acid synthase type II protein, is essential for alpha- and epoxy-mycolic acid biosynthesis and mycobacterial fitness. Sci Rep 8:6034. https://doi.org/10.1038/s41598-018-24380-5
Leger M, Gavalda S, Guillet V et al (2009) The dual function of the Mycobacterium tuberculosis FadD32 required for mycolic acid biosynthesis. Chem Biol 16:510–519. https://doi.org/10.1016/j.chembiol.2009.03.012
Lemassu A, Daffe M (1994) Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis. Biochem J 297:351–357
Lemassu A, Ortalo-Magne A, Bardou F et al (1996) Extracellular and surface-exposed polysaccharides of non-tuberculous mycobacteria. Microbiology 142:1513–1520. https://doi.org/10.1099/13500872-142-6-1513
Lennarz WJ, Talamo B (1966) The chemical characterization and enzymatic synthesis of mannolipids in Micrococcus lysodeikticus. J Biol Chem 241:2707–2719
Lerat S, Forest M, Lauzier A et al (2012) Potato suberin induces differentiation and secondary metabolism in the genus Streptomyces. Microbes Environ 27:36–42. https://doi.org/10.1264/jsme2.ME11282
Lerouge P, Lebas MH, Agapakis-Causse C, Prome JC (1988) Isolation and structural characterization of a new non-phosphorylated lipoamino acid from Mycobacterium phlei. Chem Phys Lipids 49:161–166
Letek M, Ordonez E, Vaquera J et al (2008) DivIVA is required for polar growth in the MreB-lacking rod-shaped actinomycete Corynebacterium glutamicum. J Bacteriol 190:3283–3292. https://doi.org/10.1128/JB.01934-07
Lety MA, Nair S, Berche P, Escuyer V (1997) A single point mutation in the embB gene is responsible for resistance to ethambutol in Mycobacterium smegmatis. Antimicrob Agents Chemother 41:2629–2633
Leyh-Bouille M, Bonaly R, Ghuysen JM et al (1970) LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A). Biochemistry 9:2944–2952
Li W, Xin Y, McNeil MR, Ma Y (2006) rmlB and rmlC genes are essential for growth of mycobacteria. Biochem Biophys Res Commun 342:170–178. https://doi.org/10.1016/j.bbrc.2006.01.130
Li W, Obregon-Henao A, Wallach JB et al (2016) Therapeutic potential of the Mycobacterium tuberculosis mycolic acid transporter, MmpL3. Antimicrob Agents Chemother 60:5198–5207. https://doi.org/10.1128/AAC.00826-16
Li W, Yazidi A, Pandya AN et al (2018) MmpL3 as a target for the treatment of drug-resistant nontuberculous mycobacterial infections. Front Microbiol 9:1547. https://doi.org/10.3389/fmicb.2018.01547
Linos A, Berekaa MM, Reichelt R et al (2000) Biodegradation of cis-1,4-polyisoprene rubbers by distinct actinomycetes: microbial strategies and detailed surface analysis. Appl Environ Microbiol 66:1639–1645
Liu C-W, Liu H-S (2011) Rhodococcus erythropolis strain NTU-1 efficiently degrades and traps diesel and crude oil in batch and fed-batch bioreactors. Process Biochem 46:202–209. https://doi.org/10.1016/j.procbio.2010.08.008
Logsdon MM, Aldridge BB (2018) Stable regulation of cell cycle events in mycobacteria: insights from inherently heterogeneous bacterial populations. Front Microbiol 9:514. https://doi.org/10.3389/fmicb.2018.00514
Lopez-Marin LM, Gautier N, Laneelle MA et al (1994) Structures of the glycopeptidolipid antigens of Mycobacterium abscessus and Mycobacterium chelonae and possible chemical basis of the serological cross-reactions in the Mycobacterium fortuitum complex. Microbiology 140:1109–1118
Ma Y, Mills JA, Belisle JT et al (1997) Determination of the pathway for rhamnose biosynthesis in mycobacteria: cloning, sequencing and expression of the Mycobacterium tuberculosis gene encoding alpha-d-glucose-1-phosphate thymidylyltransferase. Microbiology 143:937–945. https://doi.org/10.1099/00221287-143-3-937
Ma Y, Stern RJ, Scherman MS et al (2001) Drug targeting Mycobacterium tuberculosis cell wall synthesis: genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose. Antimicrob Agents Chemother 45:1407–1416. https://doi.org/10.1128/AAC.45.5.1407-1416.2001
Ma Y, Pan F, McNeil M (2002) Formation of dTDP-rhamnose is essential for growth of mycobacteria. J Bacteriol 184:3392–3395. https://doi.org/10.1128/JB.184.12.3392-3395.2002
Machowski EE, Senzani S, Ealand C, Kana BD (2014) Comparative genomics for mycobacterial peptidoglycan remodelling enzymes reveals extensive genetic multiplicity. BMC Microbiol 14:75. https://doi.org/10.1186/1471-2180-14-75
Madigan CA, Cambier CJ, Kelly-Scumpia KM et al (2017) A macrophage response to Mycobacterium leprae phenolic glycolipid initiates nerve damage in leprosy. Cell 170:973–985.e10. https://doi.org/10.1016/j.cell.2017.07.030
Maes E, Coddeville B, Kremer L, Guerardel Y (2007) Polysaccharide structural variability in mycobacteria: identification and characterization of phosphorylated mannan and arabinomannan. Glycoconj J 24:439–448. https://doi.org/10.1007/s10719-007-9036-1
Mainardi J-L, Villet R, Bugg TD et al (2008) Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria. FEMS Microbiol Rev 32:386–408. https://doi.org/10.1111/j.1574-6976.2007.00097.x
Makarov V, Manina G, Mikusova K et al (2009) Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science 324:801–804. https://doi.org/10.1126/science.1171583
Maloney E, Stankowska D, Zhang J et al (2009) The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides. PLoS Pathog 5:e1000534. https://doi.org/10.1371/journal.ppat.1000534.g009
Maloney E, Lun S, Stankowska D et al (2011) Alterations in phospholipid catabolism in Mycobacterium tuberculosis lysX mutant. Front Microbiol 2:19. https://doi.org/10.3389/fmicb.2011.00019
Marrakchi H, Laneelle M-A, Daffe M (2014) Mycolic acids: structures, biosynthesis, and beyond. Chem Biol 21:67–85. https://doi.org/10.1016/j.chembiol.2013.11.011
Marshall CG, Wright GD (1998) DdlN from vancomycin-producing Amycolatopsis orientalis C329.2 is a VanA homologue with d-alanyl-d-lactate ligase activity. J Bacteriol 180:5792–5795
Martinot AJ, Farrow M, Bai L et al (2016) Mycobacterial metabolic syndrome: LprG and Rv1410 regulate triacylglyceride levels, growth rate and virulence in Mycobacterium tuberculosis. PLoS Pathog 12:e1005351. https://doi.org/10.1371/journal.ppat.1005351.s013
Maslow JN, Irani VR, Lee S-H et al (2003) Biosynthetic specificity of the rhamnosyltransferase gene of Mycobacterium avium serovar 2 as determined by allelic exchange mutagenesis. Microbiology 149:3193–3202. https://doi.org/10.1099/mic.0.26565-0
Mathur M, Kolattukudy PE (1992) Molecular cloning and sequencing of the gene for mycocerosic acid synthase, a novel fatty acid elongating multifunctional enzyme, from Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. J Biol Chem 267:19388–19395
Mathur AK, Murthy PS, Saharia GS, Venkitasubramanian TA (1976) Studies on cardiolipin biosynthesis in Mycobacterium smegmatis. Can J Microbiol 22:354–358
Mattos-Guaraldi AL, Cappelli EA, Previato JO et al (1999) Characterization of surface saccharides in two Corynebacterium diphtheriae strains. FEMS Microbiol Lett 170:159–166
McNeil M, Daffe M, Brennan PJ (1990) Evidence for the nature of the link between the arabinogalactan and peptidoglycan of mycobacterial cell walls. J Biol Chem 265:18200–18206
Medjahed H, Reyrat J-M (2009) Construction of Mycobacterium abscessus defined glycopeptidolipid mutants: comparison of genetic tools. Appl Environ Microbiol 75:1331–1338. https://doi.org/10.1128/AEM.01914-08
Melzer ES, Sein CE, Chambers JJ, Siegrist MS (2018) DivIVA concentrates mycobacterial cell envelope assembly for initiation and stabilization of polar growth. Cytoskeleton (Hoboken) 75:498–507. https://doi.org/10.1002/cm.21490
Meniche X, de Sousa-d’Auria C, Van-der-Rest B et al (2008) Partial redundancy in the synthesis of the d-arabinose incorporated in the cell wall arabinan of Corynebacterineae. Microbiology 154:2315–2326. https://doi.org/10.1099/mic.0.2008/016378-0
Meniche X, Otten R, Siegrist MS et al (2014) Subpolar addition of new cell wall is directed by DivIVA in mycobacteria. Proc Natl Acad Sci USA 111:E3243–E3251. https://doi.org/10.1073/pnas.1402158111
Middlebrook G, Coleman CM, Schaefer WB (1959) Sulfolipid from virulent tubercle bacilli. Proc Natl Acad Sci USA 45:1801–1804
Mikusova K, Slayden RA, Besra GS, Brennan PJ (1995) Biogenesis of the mycobacterial cell wall and the site of action of ethambutol. Antimicrob Agents Chemother 39:2484–2489
Mikusova K, Huang H, Yagi T et al (2005) Decaprenylphosphoryl arabinofuranose, the donor of the d-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose. J Bacteriol 187:8020–8025. https://doi.org/10.1128/JB.187.23.8020-8025.2005
Mikusova K, Belanova M, Kordulakova J et al (2006) Identification of a novel galactosyl transferase involved in biosynthesis of the mycobacterial cell wall. J Bacteriol 188:6592–6598
Mills JA, Motichka K, Jucker M et al (2004) Inactivation of the mycobacterial rhamnosyltransferase, which is needed for the formation of the arabinogalactan-peptidoglycan linker, leads to irreversible loss of viability. J Biol Chem 279:43540–43546. https://doi.org/10.1074/jbc.M407782200
Minnikin DE, Patel PV, Alshamaony L, Goodfellow M (1977) Polar lipid-composition in classification of Nocardia and related bacteria. Int J Syst Bacteriol 27:104–117. https://doi.org/10.1099/00207713-27-2-104
Minnikin DE, Lee OY-C, Wu HHT et al (2015) Pathophysiological implications of cell envelope structure in Mycobacterium tuberculosis and related taxa. In: Ribon W (ed) Tuberculosis—expanding knowledge. InTech, London, UK, pp 145–175
Mishra AK, Alderwick LJ, Rittmann D et al (2007) Identification of an alpha(1→6) mannopyranosyltransferase (MptA), involved in Corynebacterium glutamicum lipomanann biosynthesis, and identification of its orthologue in Mycobacterium tuberculosis. Mol Microbiol 65:1503–1517. https://doi.org/10.1111/j.1365-2958.2007.05884.x
Mishra AK, Alderwick LJ, Rittmann D et al (2008a) Identification of a novel alpha(1→6) mannopyranosyltransferase MptB from Corynebacterium glutamicum by deletion of a conserved gene, NCgl1505, affords a lipomannan- and lipoarabinomannan-deficient mutant. Mol Microbiol 68:1595–1613. https://doi.org/10.1111/j.1365-2958.2008.06265.x
Mishra AK, Klein C, Gurcha SS et al (2008b) Structural characterization and functional properties of a novel lipomannan variant isolated from a Corynebacterium glutamicum pimB’ mutant. Antonie Van Leeuwenhoek 94:277–287. https://doi.org/10.1007/s10482-008-9243-1
Miyamoto Y, Mukai T, Nakata N et al (2006) Identification and characterization of the genes involved in glycosylation pathways of mycobacterial glycopeptidolipid biosynthesis. J Bacteriol 188:86–95. https://doi.org/10.1128/JB.188.1.86-95.2006
Miyamoto Y, Mukai T, Maeda Y et al (2007) Characterization of the fucosylation pathway in the biosynthesis of glycopeptidolipids from Mycobacterium avium complex. J Bacteriol 189:5515–5522. https://doi.org/10.1128/JB.00344-07
Miyamoto Y, Mukai T, Maeda Y et al (2008) The Mycobacterium avium complex gtfTB gene encodes a glucosyltransferase required for the biosynthesis of serovar 8-specific glycopeptidolipid. J Bacteriol 190:7918–7924. https://doi.org/10.1128/JB.00911-08
Miyamoto Y, Mukai T, Naka T et al (2010) Novel rhamnosyltransferase involved in biosynthesis of serovar 4-specific glycopeptidolipid from Mycobacterium avium complex. J Bacteriol 192:5700–5708. https://doi.org/10.1128/JB.00554-10
Moormann M, Zahringer U, Moll H et al (1997) A new glycosylated lipopeptide incorporated into the cell wall of a smooth variant of Gordona hydrophobica. J Biol Chem 272:10729–10738
Morita YS, Velasquez R, Taig E et al (2005) Compartmentalization of lipid biosynthesis in mycobacteria. J Biol Chem 280:21645–21652. https://doi.org/10.1074/jbc.M414181200
Morita YS, Sena CBC, Waller RF et al (2006) PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of phosphatidylinositol mannoside in mycobacteria. J Biol Chem 281:25143–25155. https://doi.org/10.1074/jbc.M604214200
Morita YS, Fukuda T, Sena CBC et al (2011) Inositol lipid metabolism in mycobacteria: biosynthesis and regulatory mechanisms. Biochim Biophys Acta 1810:630–641. https://doi.org/10.1016/j.bbagen.2011.03.017
Mougous JD, Petzold CJ, Senaratne RH et al (2004) Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat Struct Mol Biol 11:721–729. https://doi.org/10.1038/nsmb802
Movahedzadeh F, Smith DA, Norman RA et al (2004) The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence. Mol Microbiol 51:1003–1014
Mukherjee R, Chatterji D (2012) Glycopeptidolipids: immuno-modulators in greasy mycobacterial cell envelope. IUBMB Life 64:215–225. https://doi.org/10.1002/iub.602
Naka T, Nakata N, Maeda S et al (2011) Structure and host recognition of serotype 13 glycopeptidolipid from Mycobacterium intracellulare. J Bacteriol 193:5766–5774. https://doi.org/10.1128/JB.05412-11
Nakata N, Fujiwara N, Naka T et al (2008) Identification and characterization of two novel methyltransferase genes that determine the serotype 12-specific structure of glycopeptidolipids of Mycobacterium intracellulare. J Bacteriol 190:1064–1071. https://doi.org/10.1128/JB.01370-07
Nampoothiri KM, Hoischen C, Bathe B et al (2002) Expression of genes of lipid synthesis and altered lipid composition modulates l-glutamate efflux of Corynebacterium glutamicum. Appl Microbiol Biotechnol 58:89–96. https://doi.org/10.1007/s00253-001-0861-z
Nataraj V, Pang P-C, Haslam SM et al (2015) MKAN27435 is required for the biosynthesis of higher subclasses of lipooligosaccharides in Mycobacterium kansasii. PLoS ONE 10:e0122804. https://doi.org/10.1371/journal.pone.0122804
Naumova IB, Kuznetsov VD, Kudrina KS, Bezzubenkova AP (1980) The occurrence of teichoic acids in streptomycetes. Arch Microbiol 126:71–75
Nessar R, Reyrat J-M, Davidson LB, Byrd TF (2011) Deletion of the mmpL4b gene in the Mycobacterium abscessus glycopeptidolipid biosynthetic pathway results in loss of surface colonization capability, but enhanced ability to replicate in human macrophages and stimulate their innate immune response. Microbiology 157:1187–1195. https://doi.org/10.1099/mic.0.046557-0
Nguyen TM, Kim J (2015) Streptomyces gilvifuscus sp. nov., an actinomycete that produces antibacterial compounds isolated from soil. Int J Syst Evol Microbiol 65:3493–3500. https://doi.org/10.1099/ijsem.0.000447
Nguyen L, Scherr N, Gatfield J et al (2007) Antigen 84, an effector of pleiomorphism in Mycobacterium smegmatis. J Bacteriol 189:7896–7910. https://doi.org/10.1128/JB.00726-07
Niederweis M (2008) Nutrient acquisition by mycobacteria. Microbiology 154:679–692. https://doi.org/10.1099/mic.0.2007/012872-0
Niescher S, Wray V, Lang S et al (2006) Identification and structural characterisation of novel trehalose dinocardiomycolates from n-alkane-grown Rhodococcus opacus 1CP. Appl Microbiol Biotechnol 70:605–611. https://doi.org/10.1007/s00253-005-0113-8
Noda M, Kawahara Y, Ichikawa A et al (2004) Self-protection mechanism in d-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and d-alanyl-d-alanine ligase, which are target enzymes of d-cycloserine. J Biol Chem 279:46143–46152. https://doi.org/10.1074/jbc.M404603200
Normand P, Lapierre P, Tisa LS et al (2007) Genome characteristics of facultatively symbiotic Frankia sp. strains reflect host range and host plant biogeography. Genome Res 17:7–15. https://doi.org/10.1101/gr.5798407
Odriozola JM, Ramos JA, Bloch K (1977) Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system. Biochim Biophys Acta 488:207–217
Onwueme KC, Ferreras JA, Buglino J et al (2004) Mycobacterial polyketide-associated proteins are acyltransferases: proof of principle with Mycobacterium tuberculosis PapA5. Proc Natl Acad Sci USA 101:4608–4613. https://doi.org/10.1073/pnas.0306928101
Onwueme KC, Vos CJ, Zurita J et al (2005) Identification of phthiodiolone ketoreductase, an enzyme required for production of mycobacterial diacyl phthiocerol virulence factors. J Bacteriol 187:4760–4766. https://doi.org/10.1128/JB.187.14.4760-4766.2005
Ordway D, Henao-Tamayo M, Harton M et al (2007) The hypervirulent Mycobacterium tuberculosis strain HN878 induces a potent TH1 response followed by rapid down-regulation. J Immunol 179:522–531
Ortalo-Magne A, Dupont MA, Lemassu A et al (1995) Molecular composition of the outermost capsular material of the tubercle bacillus. Microbiology 141:1609–1620. https://doi.org/10.1099/13500872-141-7-1609
Pacheco GJ, Ciapina EMP, Gomes E de B, Junior NP (2010) Biosurfactant production by Rhodococcus erythropolis and its application to oil removal. Braz J Microbiol 41:685–693. https://doi.org/10.1590/S1517-83822010000300019
Pakkiri LS, Waechter CJ (2005) Dimannosyldiacylglycerol serves as a lipid anchor precursor in the assembly of the membrane-associated lipomannan in Micrococcus luteus. Glycobiology 15:291–302. https://doi.org/10.1093/glycob/cwi003
Pakkiri LS, Wolucka BA, Lubert EJ, Waechter CJ (2004) Structural and topological studies on the lipid-mediated assembly of a membrane-associated lipomannan in Micrococcus luteus. Glycobiology 14:73–81. https://doi.org/10.1093/glycob/cwh012
Pan F, Jackson M, Ma Y, McNeil M (2001) Cell wall core galactofuran synthesis is essential for growth of mycobacteria. J Bacteriol 183:3991–3998. https://doi.org/10.1128/JB.183.13.3991-3998.2001
Pardeshi P, Rao KK, Balaji PV (2017) Rv3634c from Mycobacterium tuberculosis H37Rv encodes an enzyme with UDP-Gal/Glc and UDP-GalNAc 4-epimerase activities. PLoS ONE 12:e0175193. https://doi.org/10.1371/journal.pone.0175193
Pasciak M, Kaczynski Z, Lindner B et al (2010) Immunochemical studies of trehalose-containing major glycolipid from Tsukamurella pulmonis. Carbohydr Res 345:1570–1574. https://doi.org/10.1016/j.carres.2010.04.026
Passeri A, Lang S, Wagner F, Wray V (1991) Marine biosurfactants, II. Production and characterization of an anionic trehalose tetraester from the marine bacterium Arthrobacter sp. EK 1. Z Naturforsch, C: J Biosci 46:204–209
Patterson JH, McConville MJ, Haites RE et al (2000) Identification of a methyltransferase from Mycobacterium smegmatis involved in glycopeptidolipid synthesis. J Biol Chem 275:24900–24906. https://doi.org/10.1074/jbc.M000147200
Peng W, Zou L, Bhamidi S et al (2012) The galactosamine residue in mycobacterial arabinogalactan is alpha-linked. J Org Chem 77:9826–9832. https://doi.org/10.1021/jo301393s
Pérez E, Constant P, Laval F et al (2004a) Molecular dissection of the role of two methyltransferases in the biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the Mycobacterium tuberculosis complex. J Biol Chem 279:42584–42592. https://doi.org/10.1074/jbc.M406134200
Pérez E, Constant P, Lemassu A et al (2004b) Characterization of three glycosyltransferases involved in the biosynthesis of the phenolic glycolipid antigens from the Mycobacterium tuberculosis complex. J Biol Chem 279:42574–42583. https://doi.org/10.1074/jbc.M406246200
Perkins HR (1971) Homoserine and diaminobutyric acid in the mucopeptide-precursor-nucleotides and cell walls of some plant-pathogenic corynebacteria. Biochem J 121:417–423
Perkins HR, Cummins CS (1964) Chemical structure of bacterial cell walls. Ornithine and 2,4-diaminobutyric acid as components of the cell walls of plant pathogenic corynebacteria. Nature 201:1105–1107
Petit JF, Adam A, Wietzerbin-Falszpan J et al (1969) Chemical structure of the cell wall of Mycobacterium smegmatis. I. Isolation and partial characterization of the peptidoglycan. Biochem Biophys Res Commun 35:478–485
Petrickova K (2003) Eukaryotic-type protein kinases in Streptomyces coelicolor: variations on a common theme. Microbiology 149:1609–1621. https://doi.org/10.1099/mic.0.26275-0
Peyret JL, Bayan N, Joliff G et al (1993) Characterization of the cspB gene encoding PS2, an ordered surface-layer protein in Corynebacterium glutamicum. Mol Microbiol 9:97–109
Philp JC, Kuyukina MS, Ivshina IB et al (2002) Alkanotrophic Rhodococcus ruber as a biosurfactant producer. Appl Microbiol Biotechnol 59:318–324. https://doi.org/10.1007/s00253-002-1018-4
Pitarque S, Larrouy-Maumus G, Payre B et al (2008) The immunomodulatory lipoglycans, lipoarabinomannan and lipomannan, are exposed at the mycobacterial cell surface. Tuberculosis (Edinb) 88:560–565. https://doi.org/10.1016/j.tube.2008.04.002
Powell DA, Duckworth M, Baddiley J (1975) A membrane-associated lipomannan in micrococci. Biochem J 151:387–397
Puech V, Chami M, Lemassu A et al (2001) Structure of the cell envelope of corynebacteria: importance of the non-covalently bound lipids in the formation of the cell wall permeability barrier and fracture plane. Microbiology 147:1365–1382. https://doi.org/10.1099/00221287-147-5-1365
Puffal J, Garcia-Heredia A, Rahlwes KC, et al (2018) Spatial control of cell envelope biosynthesis in mycobacteria. Pathog Dis 76:fty027. https://doi.org/10.1093/femspd/fty027
Qu H, Xin Y, Dong X, Ma Y (2007) An rmlA gene encoding d-glucose-1-phosphate thymidylyltransferase is essential for mycobacterial growth. FEMS Microbiol Lett 275:237–243. https://doi.org/10.1111/j.1574-6968.2007.00890.x
Quemard A (2016) New insights into the mycolate-containing compound biosynthesis and transport in mycobacteria. Trends Microbiol 24:725–738. https://doi.org/10.1016/j.tim.2016.04.009
Radmacher E, Alderwick LJ, Besra GS et al (2005) Two functional FAS-I type fatty acid synthases in Corynebacterium glutamicum. Microbiology 151:2421–2427. https://doi.org/10.1099/mic.0.28012-0
Rahlwes KC, Ha SA, Motooka D et al (2017) The cell envelope-associated phospholipid-binding protein LmeA is required for mannan polymerization in mycobacteria. J Biol Chem 292:17407–17417. https://doi.org/10.1074/jbc.M117.804377
Rahman O, Pfitzenmaier M, Pester O et al (2009) Macroamphiphilic components of thermophilic actinomycetes: identification of lipoteichoic acid in Thermobifida fusca. J Bacteriol 191:152–160. https://doi.org/10.1128/JB.01105-08
Rainczuk AK, Yamaryo-Botte Y, Brammananth R et al (2012) The lipoprotein LpqW is essential for the mannosylation of periplasmic glycolipids in corynebacteria. J Biol Chem 287:42726–42738. https://doi.org/10.1074/jbc.M112.373415
Rainwater DL, Kolattukudy PE (1983) Synthesis of mycocerosic acids from methylmalonyl coenzyme A by cell-free extracts of Mycobacterium tuberculosis var. bovis BCG. J Biol Chem 258:2979–2985
Rainwater DL, Kolattukudy PE (1985) Fatty acid biosynthesis in Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin. Purification and characterization of a novel fatty acid synthase, mycocerosic acid synthase, which elongates n-fatty acyl-CoA with methylmalonyl-CoA. J Biol Chem 260:616–623
Ramos A, Honrubia MP, Valbuena N et al (2003) Involvement of DivIVA in the morphology of the rod-shaped actinomycete Brevibacterium lactofermentum. Microbiology 149:3531–3542. https://doi.org/10.1099/mic.0.26653-0
Rana AK, Singh A, Gurcha SS et al (2012) Ppm1-encoded polyprenyl monophosphomannose synthase activity is essential for lipoglycan synthesis and survival in mycobacteria. PLoS ONE 7:e48211. https://doi.org/10.1371/journal.pone.0048211
Rao A, Ranganathan A (2004) Interaction studies on proteins encoded by the phthiocerol dimycocerosate locus of Mycobacterium tuberculosis. Mol Genet Genomics 272:571–579. https://doi.org/10.1007/s00438-004-1088-3
Recht J, Kolter R (2001) Glycopeptidolipid acetylation affects sliding motility and biofilm formation in Mycobacterium smegmatis. J Bacteriol 183:5718–5724. https://doi.org/10.1128/JB.183.19.5718-5724.2001
Recht J, Martinez A, Torello S, Kolter R (2000) Genetic analysis of sliding motility in Mycobacterium smegmatis. J Bacteriol 182:4348–4351
Reed MB, Domenech P, Manca C et al (2004) A glycolipid of hypervirulent tuberculosis strains that inhibits the innate immune response. Nature 431:84–87. https://doi.org/10.1038/nature02837
Ren H, Dover LG, Islam ST et al (2007) Identification of the lipooligosaccharide biosynthetic gene cluster from Mycobacterium marinum. Mol Microbiol 63:1345–1359. https://doi.org/10.1111/j.1365-2958.2007.05603.x
Ripoll F, Deshayes C, Pasek S, et al (2007) Genomics of glycopeptidolipid biosynthesis in Mycobacterium abscessus and M. chelonae. BMC Genomics 8:114. https://doi.org/10.1186/1471-2164-8-114
Rojas ER, Billings G, Odermatt PD et al (2018) The outer membrane is an essential load-bearing element in Gram-negative bacteria. Nature 559:617–621. https://doi.org/10.1038/s41586-018-0344-3
Rombouts Y, Burguiere A, Maes E et al (2009) Mycobacterium marinum lipooligosaccharides are unique caryophyllose-containing cell wall glycolipids that inhibit tumor necrosis factor-alpha secretion in macrophages. J Biol Chem 284:20975–20988. https://doi.org/10.1074/jbc.M109.011429
Rombouts Y, Elass E, Biot C et al (2010) Structural analysis of an unusual bioactive N-acylated lipo-oligosaccharide LOS-IV in Mycobacterium marinum. J Am Chem Soc 132:16073–16084. https://doi.org/10.1021/ja105807s
Rombouts Y, Alibaud L, Carrere-Kremer S et al (2011) Fatty acyl chains of Mycobacterium marinum lipooligosaccharides: structure, localization and acylation by PapA4 (MMAR_2343) protein. J Biol Chem 286:33678–33688. https://doi.org/10.1074/jbc.M111.273920
Rousseau C, Neyrolles O, Bordat Y et al (2003) Deficiency in mycolipenate- and mycosanoate-derived acyltrehaloses enhances early interactions of Mycobacterium tuberculosis with host cells. Cell Microbiol 5:405–415
Saadat S, Ballou CE (1983) Pyruvylated glycolipids from Mycobacterium smegmatis. Structures of two oligosaccharide components. J Biol Chem 258:1813–1818
Sambou T, Dinadayala P, Stadthagen G et al (2008) Capsular glucan and intracellular glycogen of Mycobacterium tuberculosis: biosynthesis and impact on the persistence in mice. Mol Microbiol 70:762–774. https://doi.org/10.1111/mmi.2008.70.issue-3
Sanders AN, Wright LF, Pavelka MS (2014) Genetic characterization of mycobacterial L,D-transpeptidases. Microbiology 160:1795–1806. https://doi.org/10.1099/mic.0.078980-0
Sandoval-Calderon M, Geiger O, Guan Z et al (2009) A eukaryote-like cardiolipin synthase is present in Streptomyces coelicolor and in most Actinobacteria. J Biol Chem 284:17383–17390. https://doi.org/10.1074/jbc.M109.006072
Sandoval-Calderon M, Nguyen DD, Kapono CA et al (2015) Plasticity of Streptomyces coelicolor membrane composition under different growth conditions and during development. Front Microbiol 6:1465. https://doi.org/10.3389/fmicb.2015.01465
Sani M, Houben ENG, Geurtsen J et al (2010) Direct visualization by cryo-EM of the mycobacterial capsular layer: a labile structure containing Esx-1-secreted proteins. PLoS Pathog 6:e1000794. https://doi.org/10.1371/journal.ppat.1000794.t001
Sarkar D, Sidhu M, Singh A et al (2011) Identification of a glycosyltransferase from Mycobacterium marinum involved in addition of a caryophyllose moiety in lipooligosaccharides. J Bacteriol 193:2336–2340. https://doi.org/10.1128/JB.00065-11
Schelle MW, Bertozzi CR (2006) Sulfate metabolism in mycobacteria. ChemBioChem 7:1516–1524. https://doi.org/10.1002/cbic.200600224
Scher M, Lennarz WJ (1969) Studies on the biosynthesis of mannan in Micrococcus lysodeikticus. I. Characterization of mannan-14C formed enzymatically from mannosyl-1-phosphoryl-undecaprenol. J Biol Chem 244:2777–2789
Scherman M, Weston A, Duncan K et al (1995) Biosynthetic origin of mycobacterial cell wall arabinosyl residues. J Bacteriol 177:7125–7130
Schleifer KH, Kandler O (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36:407–477
Schoonmaker MK, Bishai WR, Lamichhane G (2014) Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell size, morphology, the cytosolic matrix, protein localization, virulence, and resistance to beta-lactams. J Bacteriol 196:1394–1402. https://doi.org/10.1128/JB.01396-13
Schorey JS, Sweet L (2008) The mycobacterial glycopeptidolipids: structure, function, and their role in pathogenesis. Glycobiology 18:832–841. https://doi.org/10.1093/glycob/cwn076
Seeliger JC, Holsclaw CM, Schelle MW, et al (2011) Elucidation and chemical modulation of sulfolipid-1 biosynthesis in Mycobacterium tuberculosis. J Biol Chem. https://doi.org/10.1074/jbc.m111.315473
Seidel M, Alderwick LJ, Birch HL et al (2007) Identification of a novel arabinofuranosyltransferase AftB involved in a terminal step of cell wall arabinan biosynthesis in Corynebacterianeae, such as Corynebacterium glutamicum and Mycobacterium tuberculosis. J Biol Chem 282:14729–14740. https://doi.org/10.1074/jbc.M700271200
Selim MS, Amer SK, Mohamed SS et al (2018) Production and characterisation of exopolysaccharide from Streptomyces carpaticus isolated from marine sediments in Egypt and its effect on breast and colon cell lines. J Genet Eng Biotechnol 16:23–28. https://doi.org/10.1016/j.jgeb.2017.10.014
Sena CBC, Fukuda T, Miyanagi K et al (2010) Controlled expression of branch-forming mannosyltransferase is critical for mycobacterial lipoarabinomannan biosynthesis. J Biol Chem 285:13326–13336. https://doi.org/10.1074/jbc.M109.077297
Senzani S, Li D, Bhaskar A et al (2017) An amidase_3 domain-containing N-acetylmuramyl-l-alanine amidase is required for mycobacterial cell division. Sci Rep 7:1140. https://doi.org/10.1038/s41598-017-01184-7
Severn WB, Richards JC (1992) The acidic specific capsular polysaccharide of Rhodococcus equi serotype 3. Structural elucidation and stereochemical analysis of the lactate ether and pyruvate acetal substituents. Can J Chem 70:2664–2676. https://doi.org/10.1139/v92-336
Shi L, Berg S, Lee A et al (2006) The carboxy terminus of EmbC from Mycobacterium smegmatis mediates chain length extension of the arabinan in lipoarabinomannan. J Biol Chem 281:19512–19526. https://doi.org/10.1074/jbc.M513846200
Simeone R, Constant P, Malaga W et al (2007) Molecular dissection of the biosynthetic relationship between phthiocerol and phthiodiolone dimycocerosates and their critical role in the virulence and permeability of Mycobacterium tuberculosis. FEBS J 274:1957–1969. https://doi.org/10.1111/j.1742-4658.2007.05740.x
Simeone R, Leger M, Constant P et al (2010) Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis. FEBS J 277:2715–2725. https://doi.org/10.1111/j.1742-464X.2010.07688.x
Singer ME, Finnerty WR, Tunelid A (1990) Physical and chemical properties of a biosurfactant synthesized by Rhodococcus species H13-A. Can J Microbiol 36:746–750. https://doi.org/10.1139/m90-128
Sirakova TD, Thirumala AK, Dubey VS et al (2001) The Mycobacterium tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J Biol Chem 276:16833–16839. https://doi.org/10.1074/jbc.M011468200
Skovierova H, Larrouy-Maumus G, Zhang J et al (2009) AftD, a novel essential arabinofuranosyltransferase from mycobacteria. Glycobiology 19:1235–1247. https://doi.org/10.1093/glycob/cwp116
Slama N, Jamet S, Frigui W et al (2016) The changes in mycolic acid structures caused by hadC mutation have a dramatic effect on the virulence of Mycobacterium tuberculosis. Mol Microbiol 99:794–807. https://doi.org/10.1111/mmi.13266
Slayden RA, Barry CE (2002) The role of KasA and KasB in the biosynthesis of meromycolic acids and isoniazid resistance in Mycobacterium tuberculosis. Tuberculosis 82:149–160
Sonden B, Kocincova D, Deshayes C et al (2005) Gap, a mycobacterial specific integral membrane protein, is required for glycolipid transport to the cell surface. Mol Microbiol 58:426–440. https://doi.org/10.1111/j.1365-2958.2005.04847.x
Stern RJ, Lee TY, Lee TJ et al (1999) Conversion of dTDP-4-keto-6-deoxyglucose to free dTDP-4-keto-rhamnose by the rmIC gene products of Escherichia coli and Mycobacterium tuberculosis. Microbiology 145:663–671. https://doi.org/10.1099/13500872-145-3-663
Stokes RW, Norris-Jones R, Brooks DE et al (2004) The glycan-rich outer layer of the cell wall of Mycobacterium tuberculosis acts as an antiphagocytic capsule limiting the association of the bacterium with macrophages. Infect Immun 72:5676–5686. https://doi.org/10.1128/IAI.72.10.5676-5686.2004
Sulzenbacher G, Canaan S, Bordat Y et al (2006) LppX is a lipoprotein required for the translocation of phthiocerol dimycocerosates to the surface of Mycobacterium tuberculosis. EMBO J 25:1436–1444. https://doi.org/10.1038/sj.emboj.7601048
Sydor T, von Bargen K, Becken U et al (2008) A mycolyl transferase mutant of Rhodococcus equi lacking capsule integrity is fully virulent. Vet Microbiol 128:327–341. https://doi.org/10.1016/j.vetmic.2007.10.020
Szczepina MG, Zheng RB, Completo GC et al (2009) STD-NMR studies suggest that two acceptor substrates for GlfT2, a bifunctional galactofuranosyltransferase required for the biosynthesis of Mycobacterium tuberculosis arabinogalactan, compete for the same binding site. ChemBioChem 10:2052–2059. https://doi.org/10.1002/cbic.200900202
Takayama K, Kilburn JO (1989) Inhibition of synthesis of arabinogalactan by ethambutol in Mycobacterium smegmatis. Antimicrob Agents Chemother 33:1493–1499
Tatituri RVV, Illarionov PA, Dover LG et al (2007) Inactivation of Corynebacterium glutamicum NCgl0452 and the role of MgtA in the biosynthesis of a novel mannosylated glycolipid involved in lipomannan biosynthesis. J Biol Chem 282:4561–4572. https://doi.org/10.1074/jbc.M608695200
Telenti A, Philipp WJ, Sreevatsan S et al (1997) The emb operon, a gene cluster of Mycobacterium tuberculosis involved in resistance to ethambutol. Nat Med 3:567–570
Thakur M, Chakraborti PK (2008) Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis. Biochem J 415:27–33. https://doi.org/10.1042/BJ20080234
Thanky NR, Young DB, Robertson BD (2007) Unusual features of the cell cycle in mycobacteria: polar-restricted growth and the snapping-model of cell division. Tuberculosis 87:231–236. https://doi.org/10.1016/j.tube.2006.10.004
Tokumoto Y, Nomura N, Uchiyama H et al (2009) Structural characterization and surface-active properties of a succinoyl trehalose lipid produced by Rhodococcus sp. SD-74. J Oleo Sci 58:97–102
Touchette MH, Holsclaw CM, Previti ML et al (2014) The rv1184c locus encodes Chp2, an acyltransferase in Mycobacterium tuberculosis polyacyltrehalose lipid biosynthesis. J Bacteriol 197:201–210. https://doi.org/10.1128/JB.02015-14
Touchette MH, Van Vlack ER, Bai L et al (2017) A screen for protein-protein interactions in live mycobacteria reveals a functional link between the virulence-associated lipid transporter lprg and the mycolyltransferase Antigen 85A. ACS Infect Dis 3:336–348. https://doi.org/10.1021/acsinfecdis.6b00179
Trivedi OA, Arora P, Sridharan V et al (2004) Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428:441–445. https://doi.org/10.1038/nature02384
Trivedi OA, Arora P, Vats A et al (2005) Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol Cell 17:631–643. https://doi.org/10.1016/j.molcel.2005.02.009
Tuleva B, Christova N, Cohen R et al (2008) Production and structural elucidation of trehalose tetraesters (biosurfactants) from a novel alkanothrophic Rhodococcus wratislaviensis strain. J Appl Microbiol 104:1703–1710. https://doi.org/10.1111/j.1365-2672.2007.03680.x
Tuleva B, Christova N, Cohen R et al (2009) Isolation and characterization of trehalose tetraester biosurfactants from a soil strain Micrococcus luteus BN56. Process Biochem 44:135–141. https://doi.org/10.1016/j.procbio.2008.09.016
Tul’skaya EM, Shashkov AS, Streshinskaya GM et al (2011) Teichuronic and teichulosonic acids of actinomycetes. Biochemistry (Moscow) 76:736–744. https://doi.org/10.1134/S0006297911070030
Turner J, Torrelles JB (2018) Mannose-capped lipoarabinomannan in Mycobacterium tuberculosis pathogenesis. Pathog Dis 76:S1130. https://doi.org/10.1093/femspd/fty026
Uchida Y, Tsuchiya R, Chino M et al (1989) Extracellular accumulation of mono- and di-succinoyl trehalose lipids by a strain of Rhodococcus erythropolis grown on n-alkanes. Agric Biol Chem 53:757–763. https://doi.org/10.1271/bbb1961.53.757
Udou T, Ogawa M, Mizuguchi Y (1983) An improved method for the preparation of mycobacterial spheroplasts and the mechanism involved in the reversion to bacillary form: electron microscopic and physiological study. Can J Microbiol 29:60–68
Vadrevu IS, Lofton H, Sarva K et al (2011) ChiZ levels modulate cell division process in mycobacteria. Tuberculosis (Edinb) 91(Suppl 1):S128–S135. https://doi.org/10.1016/j.tube.2011.10.022
van der Wel N, Hava D, Houben D et al (2007) M. tuberculosis and M. leprae translocate from the phagolysosome to the cytosol in myeloid cells. Cell 129:1287–1298. https://doi.org/10.1016/j.cell.2007.05.059
van der Woude AD, Sarkar D, Bhatt A et al (2012) Unexpected link between lipooligosaccharide biosynthesis and surface protein release in Mycobacterium marinum. J Biol Chem 287:20417–20429. https://doi.org/10.1074/jbc.M111.336461
van Straaten KE, Kuttiyatveetil JRA, Sevrain CM et al (2015) Structural basis of ligand binding to UDP-galactopyranose mutase from Mycobacterium tuberculosis using substrate and tetrafluorinated substrate analogues. J Am Chem Soc 137:1230–1244. https://doi.org/10.1021/ja511204p
Varela C, Rittmann D, Singh A et al (2012) MmpL genes are associated with mycolic acid metabolism in mycobacteria and corynebacteria. Chem Biol 19:498–506. https://doi.org/10.1016/j.chembiol.2012.03.006
Veerkamp JH (1971) The structure of the cell wall peptidoglycan of Bifidobacterium bifidum var. pennsylvanicus. Arch Biochem Biophys 143:204–211
Vences-Guzman MA, Geiger O, Sohlenkamp C (2012) Ornithine lipids and their structural modifications: from A to E and beyond. FEMS Microbiol Lett 335:1–10. https://doi.org/10.1111/j.1574-6968.2012.02623.x
Verma V, Qazi GN, Parshad R, Chopra CL (1989) A fast spheroplast formation procedure in some 2,5-diketo-d-gluconate- and 2-keto-l-gulonate-producing bacteria. Biotechniques 7:449–452
Viljoen A, Herrmann J-L, Onajole OK et al (2017) Controlling extra- and intramacrophagic Mycobacterium abscessus by targeting mycolic acid transport. Front Cell Infect Microbiol 7:388. https://doi.org/10.3389/fcimb.2017.00388
Vollbrecht E, Heckmann R, Wray V et al (1998) Production and structure elucidation of di- and oligosaccharide lipids (biosurfactants) from Tsukamurella sp. nov. Appl Microbiol Biotechnol 50:530–537
Vollmer W, Blanot D, de Pedro MA (2008) Peptidoglycan structure and architecture. FEMS Microbiol Rev 32:149–167. https://doi.org/10.1111/j.1574-6976.2007.00094.x
von Wintzingerode F, Gobel UB, Siddiqui RA et al (2001) Salana multivorans gen. nov., sp. nov., a novel actinobacterium isolated from an anaerobic bioreactor and capable of selenate reduction. Int J Syst Evol Microbiol 51:1653–1661. https://doi.org/10.1099/00207713-51-5-1653
Waddell SJ, Chung GA, Gibson KJC et al (2005) Inactivation of polyketide synthase and related genes results in the loss of complex lipids in Mycobacterium tuberculosis H37Rv. Lett Appl Microbiol 40:201–206. https://doi.org/10.1111/j.1472-765X.2005.01659.x
Wang L-Y, Li S-T, Li Y (2003) Identification and characterization of a new exopolysaccharide biosynthesis gene cluster from Streptomyces. FEMS Microbiol Lett 220:21–27. https://doi.org/10.1016/S0378-1097(03)00044-2
Wang Q, Zhu L, Jones V et al (2015) CpsA, a LytR-CpsA-Psr family protein in Mycobacterium marinum, is required for cell wall integrity and virulence. Infect Immun 83:2844–2854. https://doi.org/10.1128/IAI.03081-14
Wehmeier S, Varghese AS, Gurcha SS et al (2009) Glycosylation of the phosphate binding protein, PstS, in Streptomyces coelicolor by a pathway that resembles protein O-mannosylation in eukaryotes. Mol Microbiol 71:421–433. https://doi.org/10.1111/j.1365-2958.2008.06536.x
Weidenmaier C, Peschel A (2008) Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nat Rev Microbiol 6:276–287. https://doi.org/10.1038/nrmicro1861
Welby-Gieusse M, Laneelle MA, Asselineau J (1970) Structure of the corynomycolic acids of Corynebacterium hofmanii and their biogenetic implication. Eur J Biochem 13:164–167
Wesener DA, Levengood MR, Kiessling LL (2017) Comparing galactan biosynthesis in Mycobacterium tuberculosis and Corynebacterium diphtheriae. J Biol Chem 292:2944–2955. https://doi.org/10.1074/jbc.M116.759340
Weston A, Stern RJ, Lee RE et al (1997) Biosynthetic origin of mycobacterial cell wall galactofuranosyl residues. Tuber Lung Dis 78:123–131
Wheatley RW, Zheng RB, Richards MR et al (2012) Tetrameric structure of the GlfT2 galactofuranosyltransferase reveals a scaffold for the assembly of mycobacterial arabinogalactan. J Biol Chem 287:28132–28143. https://doi.org/10.1074/jbc.M112.347484
White DA, Hird LC, Ali ST (2013) Production and characterization of a trehalolipid biosurfactant produced by the novel marine bacterium Rhodococcus sp., strain PML026. J Appl Microbiol 115:744–755. https://doi.org/10.1111/jam.12287
Wietzerbin J, Das BC, Petit JF et al (1974) Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of mycobacteria. Biochemistry 13:3471–3476
Wolucka BA, de Hoffmann E (1995) The presence of beta-d-ribosyl-1-monophosphodecaprenol in mycobacteria. J Biol Chem 270:20151–20155
Wolucka BA, McNeil MR, de Hoffmann E et al (1994) Recognition of the lipid intermediate for arabinogalactan/arabinomannan biosynthesis and its relation to the mode of action of ethambutol on mycobacteria. J Biol Chem 269:23328–23335
World Health Organization (2018) Global tuberculosis report 2018, pp 1–277
Xin Y, Lee RE, Scherman MS et al (1997) Characterization of the in vitro synthesized arabinan of mycobacterial cell walls. Biochim Biophys Acta 1335:231–234
Xu Z, Meshcheryakov VA, Poce G, Chng S-S (2017) MmpL3 is the flippase for mycolic acids in mycobacteria. Proc Natl Acad Sci USA 114:7993–7998. https://doi.org/10.1073/pnas.1700062114
Yague P, Willemse J, Koning RI et al (2016) Subcompartmentalization by cross-membranes during early growth of Streptomyces hyphae. Nat Commun 7:12467. https://doi.org/10.1038/ncomms12467
Yakimov MM, Giuliano L, Bruni V et al (1999) Characterization of antarctic hydrocarbon-degrading bacteria capable of producing bioemulsifiers. New Microbiol 22:249–256
Yamaryo-Botte Y, Rainczuk AK, Lea-Smith DJ, et al (2014) Acetylation of trehalose mycolates is required for efficient MmpL-mediated membrane transport in Corynebacterineae. ACS Chem Biol 141209130005000. https://doi.org/10.1021/cb5007689
Yano I, Furukawa Y, Kusunose M (1969) Phospholipids of Nocardia coeliaca. J Bacteriol 98:124–130
Zanfardino A, Migliardi A, D’Alonzo D et al (2016) Inactivation of MSMEG_0412 gene drastically affects surface related properties of Mycobacterium smegmatis. BMC Microbiol 16:267. https://doi.org/10.1186/s12866-016-0888-z
Zhang N, Torrelles JB, McNeil MR et al (2003) The Emb proteins of mycobacteria direct arabinosylation of lipoarabinomannan and arabinogalactan via an N-terminal recognition region and a C-terminal synthetic region. Mol Microbiol 50:69–76
Zheng H, Lu L, Wang B et al (2008) Genetic basis of virulence attenuation revealed by comparative genomic analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv. PLoS ONE 3:e2375. https://doi.org/10.1371/journal.pone.0002375
Zhou X, Halladin DK, Theriot JA (2016) Fast mechanically driven daughter cell separation is widespread in Actinobacteria. mBio 7:e00952–16-6. https://doi.org/10.1128/mbio.00952-16
Zhou X, Rodriguez-Rivera FP, Lim HC et al (2019) Sequential assembly of the septal cell envelope prior to V snapping in Corynebacterium glutamicum. Nat Chem Biol 2:a000414. https://doi.org/10.1038/s41589-018-0206-1
Zuber B, Chami M, Houssin C et al (2008) Direct visualization of the outer membrane of mycobacteria and corynebacteria in their native state. J Bacteriol 190:5672–5680. https://doi.org/10.1128/JB.01919-07
Zuneda MC, Guillenea JJ, Dominguez JB et al (1984) Lipid composition and protoplast-forming capacity of Streptomyces antibioticus. Lipids 19:223–228
Acknowledgements
The authors thank Julia Puffal, Corelle Rokicki and James Brenner for discussions. The recent work in our laboratory was supported by the American Lung Association, Pittsfield Anti-Tuberculosis Association, and NIH (AI140259).
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Rahlwes, K.C., Sparks, I.L., Morita, Y.S. (2019). Cell Walls and Membranes of Actinobacteria. In: Kuhn, A. (eds) Bacterial Cell Walls and Membranes . Subcellular Biochemistry, vol 92. Springer, Cham. https://doi.org/10.1007/978-3-030-18768-2_13
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