Abstract
Mycoplasma pneumoniae synthesizes a complex polar structure,the attachment organelle (AO), which is required for productive adherence to host cells. Because in natureM. pneumoniae cannot survive outside the host, this structure is essentialto the M. pneumoniae cell. While it is understood that the AO is thesite at which adhesin proteins are concentrated, how that localization is mediated is unknown. However,the presence at the AO of a set of novel, detergent-insoluble proteins and structures which are indirectlyrequired for normal function of this structure has provided insight into its assembly and architecture.Biochemical, genetic, and immunocytochemical studies of these cytadherence-accessory proteins and theirinterrelationships have revealed remarkable complexity in this supposedly minimal bacterial cell.
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References
Balish MF, Hahn TW, Popham PL, Krause DC (2001) Stability of Mycoplasma pneumoniae cytadherence-accessory protein HMW1 correlates with its association with the triton shell. J Bacteriol 183:3680–3688
Balish MF, Krause DC (2002) Cytadherence and the cytoskeleton. In: Razin S, Herrmann R (eds) Molecular biology and pathogenesis of mycoplasmas. Kluwer Academic/Plenum Publishers, New York, pp 491–518
Balish MF, Ross SM, Fisseha M, Krause DC (2003a) Deletion analysis identifies key functional domains of the cytadherence-associated protein HMW2 of Mycoplasma pneumoniae. Mol Microbiol 50:1507–1516
Balish MF, Santurri RT, Ricci AM, Lee KK, Krause DC (2003b) Localization of Mycoplasma pneumoniae cytadherence-associated protein HMW2 by fusion with green fluorescent protein: implications for attachment organelle structure. Mol Microbiol 47:49–60
Baseman JB, Cole RM, Krause DC, Leith DK (1982) Molecular basis for cytadsorption of Mycoplasma pneumoniae. J Bacteriol 151:1514–1522
Baseman JB, Morrison-Plummer J, Drouillard D, Puleo-Scheppke B, Tryon V, Holt SC (1987) Identification of a 32-kilodalton protein of Mycoplasma pneumoniae associated with hemadsorption. Isr J Med Sci 23:474–479
Biberfeld G, Biberfeld P (1970) Ultrastructural features of Mycoplasma pneumoniae. J Bacteriol 102:855–861
Bredt W (1968) Motility and multiplication of Mycoplasma pneumoniae. A phase contrast study. Pathol Microbiol 32:321–326
Collier AM, Clyde WA Jr (1971) Relationships between Mycoplasma pneumoniae and human respiratory epithelium. Infect Immun 3:694–701
Collier AM, Hu PC, Clyde WA Jr (1983) Location of attachment moiety on Mycoplasma pneumoniae. Yale J Biol Med 56:671–677
Feldner J, Gobel U, Bredt W (1982) Mycoplasma pneumoniae adhesin localized to tip structure by monoclonal antibody. Nature 298:765–767
Gobel U, Speth V, Bredt W (1981) Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J Cell Biol 91:537–543
Hansen EJ, Wilson RM, Baseman JB (1979) Isolation of mutants of Mycoplasma pneumoniae defective in hemadsorption. Infect Immun 23:903–906
Hegermann J, Herrmann R, Mayer F (2002) Cytoskeletal elements in the bacterium Mycoplasma pneumoniae. Naturwissenschaften 89:453–458
Hu PC, Collier AM, Baseman JB (1977) Surface parasitism by Mycoplasma pneumoniae of respiratory epithelium. J Exp Med 145:1328–1343
Jordan JL, Berry KM, Balish MF, Krause DC (2001) Stability and subcellular localization of cytadherence-associated protein P65 in Mycoplasma pneumoniae. J Bacteriol 183:7387–7391
Kenri T, Seto S, Horino A, Sasaki Y, Sasaki T, Miyata M (2004) Use of fluorescent-protein tagging to determine the subcellular localization of Mycoplasma pneumoniae proteins encoded by the cytadherence regulatory locus. J Bacteriol 186:6944–6955
Krause DC, Balish MF (2004) Cellular engineering in a minimal microbe: structure and assembly of the terminal organelle of Mycoplasma pneumoniae. Mol Microbiol 51:917–924
Krause DC, Leith DK, Baseman JB (1983) Reacquisition of specific proteins confers virulence in Mycoplasma pneumoniae. Infect Immun 39:830–836
Krause DC, Leith DK, Wilson RM, Baseman JB (1982) Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence. Infect Immun 35:809–817
Krause DC, Proft T, Hedreyda CT, Hilbert H, Plagens H, Herrmann R (1997) Transposon mutagenesis reinforces the correlation between Mycoplasma pneumoniae cytoskeletal protein HMW2 and cytadherence. J Bacteriol 179:2668–2677
Layh-Schmitt G, Harkenthal M (1999) The 40 and 90kDa membrane proteins (ORF6 gene product) of Mycoplasma pneumoniae are responsible for the tip structure formation and P1 (adhesin) association with the Triton shell. FEMS Microbiol Lett 174:143–149
Layh-Schmitt G, Herrmann R (1992) Localization and biochemical characterization of the ORF6 gene product of the Mycoplasma pneumoniae P1 operon. Infect Immun 60:2906–2913
Layh-Schmitt G, Herrmann R (1994) Spatial arrangement of gene products of the P1 operon in the membrane of Mycoplasma pneumoniae. Infect Immun 62:974–979
Layh-Schmitt G, Podtelejnikov A, Mann M (2000) Proteins complexed to the P1 adhesin of Mycoplasma pneumoniae. Microbiology 146:741–747
Lipman RP, Clyde WA Jr, Denny FW (1969) Characteristics of virulent, attenuated, and avirulent Mycoplasma pneumoniae strains. J Bacteriol 100:1037–1043
Meng KE, Pfister RM (1980) Intracellular structure of Mycoplasma pneumoniae revealed after membrane removal. J Bacteriol 144:390–399
Morrison-Plummer J, Leith DK, Baseman JB (1986) Biological effects of anti-lipid and anti-protein monoclonal antibodies on Mycoplasma pneumoniae. Infect Immun 53:398–403
Popham PL, Hahn TW, Krebes KA, Krause DC (1997) Loss of HMW1 and HMW3 in noncytadhering mutants of Mycoplasma pneumoniae occurs post-translationally. Proc Natl Acad Sci USA 94:13979–13984
Proft T, Hilbert H, Layh-Schmitt G, Herrmann R (1995) The proline-rich P65 protein of Mycoplasma pneumoniae is a component of the Triton X-100-insoluble fraction and exhibits size polymorphism in the strains M129 and FH. J Bacteriol 177:3370–3378
Regula JT, Boguth G, Gorg A, Hegermann J, Mayer F, Frank R, Herrmann R (2001) Defining the mycoplasma ‘cytoskeleton’: the protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2D gel electrophoresis and mass spectrometry. Microbiology 147:1045–1057
Romero-Arroyo CE, Jordan J, Peacock SJ, Willby MJ, Farmer MA, Krause DC (1999) Mycoplasma pneumoniae protein P30 is required for cytadherence and associated with proper cell development. J Bacteriol 181:1079–1087
Seto S, Layh-Schmitt G, Kenri T, Miyata M (2001) Visualization of the attachment organelle and cytadherence proteins of Mycoplasma pneumoniae by immunofluorescence microscopy. J Bacteriol 183:1621–1630
Seto S, Miyata M (2003) Attachment organelle formation represented by localization of cytadherence proteins and formation of the electron-dense core in wild-type and mutant strains of Mycoplasma pneumoniae. J Bacteriol 185:1082–1091
Sobeslavsky O, Prescott B, Chanock RM (1968) Adsorption of Mycoplasma pneumoniae to neuraminic acid receptors of various cells and possible role in virulence. J Bacteriol 96:695–705
Sperker B, Hu P, Herrmann R (1991) Identification of gene products of the P1 operon of Mycoplasma pneumoniae. Mol Microbiol 5:299–306
Stevens MK, Krause DC (1991) Localization of the Mycoplasma pneumoniae cytadherence-accessory proteins HMW1 and HMW4 in the cytoskeletonlike Triton shell. J Bacteriol 173:1041–1050
Stevens MK, Krause DC (1992) Mycoplasma pneumoniae cytadherence phase-variable protein HMW3 is a component of the attachment organelle. J Bacteriol 174:4265–4274
Su CJ, Tryon VV, Baseman JB (1987) Cloning and sequence analysis of cytadhesin P1 from Mycoplasma pneumoniae. Infect Immun 55:3023–3029
Waites KB, Talkington DF (2004) Mycoplasma pneumoniae and its role as a human pathogen. Clin Microbiol Rev 17:697–728
Waldo RH III, Jordan JL, Krause DC (2005) Identification and complementation of a mutation associated with loss of Mycoplasma pneumoniae virulence-specific proteins B and C. J Bacteriol 187:747–751
Willby MJ, Balish MF, Ross SM, Lee KK, Jordan JL, Krause DC (2004) HMW1 is required for stability and localization of HMW2 to the attachment organelle of Mycoplasma pneumoniae. J Bacteriol 186:8221–8228
Willby MJ, Krause DC (2002) Characterization of a Mycoplasma pneumoniae hmw3 mutant: implications for attachment organelle assembly. J Bacteriol 184:3061–3068
Acknowledgments
I thank J. Hatchel, M. Duley, S. Ross, and D. Krause for providing electron micrographs. This work was supported by Miami University startup funds.
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Balish, M.F. (2006). Organization and Assembly of the Mycoplasma pneumoniae Attachment Organelle. In: Shively, J.M. (eds) Complex Intracellular Structures in Prokaryotes. Microbiology Monographs, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/7171_031
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DOI: https://doi.org/10.1007/7171_031
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