Abstract
Chitin-containing organisms, such as fungi and arthropods, use chitin as a structural component to protect themselves from harsh environmental conditions. Hosts such as mammals and plants, however, sense chitin to initiate innate and adaptive immunity and exclude chitin-containing organisms. A number of protein factors are then expressed, and several signaling pathways are triggered. In this chapter, we focus on the responses and signal transduction pathways that are activated in mammals and plants upon invasion by chitin-containing organisms. As host chitinases play important roles in the glycolytic processing of chitin, which is then recognized by pattern-recognition receptors, we also pay special attention to the chitinases that are involved in immune recognition.
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Abbreviations
- Arg1:
-
Arginase 1
- CCL2:
-
chemokine (C-C motif) ligand 2
- CD11:
-
cluster of differentiation 11
- CXCL8:
-
chemokine (C-X-C motif) ligand 8
- ECD:
-
ectodomain
- EF-Tu:
-
elongation factor thermo unstable
- FIBCD1:
-
fibrinogen C domain containing 1
- Fizz1:
-
found in inflammatory zone 1
- flg22:
-
flagelin 22
- HDM:
-
house dust mite
- GlcNAc:
-
2-acetamido-2-deoxy-D-glucopyranose
- IL:
-
interleukin
- LRR:
-
leucine-rich repeat
- LTD4:
-
leukotriene D4
- MALT1:
-
mucosa-associated lymphoid tissue lymphoma translocation protein 1
- MAPK:
-
mitogen-activated protein kinase
- MPK3:
-
mitogen-activated protein kinase 3
- MyD88:
-
myeloid differentiation factor 88
- M2:
-
alternatively activated macrophages
- (NAG)n:
-
β-1,4-linked oligosaccharide of GlcNAc with a polymerization degree of n
- NMR:
-
nuclear magnetic resonance
- NOD2:
-
nucleotide-binding oligomerization domain-containing protein 2
- PAMPs:
-
pathogen-associated molecular patterns
- PGD2:
-
prostaglandin D2
- PRRs:
-
pattern-recognition receptors
- RLCK:
-
receptor-like cytoplasmic kinase
- ROS:
-
reactive oxygen species
- TLR:
-
toll-like receptor
- TNF:
-
tumor necrosis factor
- TSLP:
-
thymic stromal lymphopoietin
- WRKY:
-
transcription factor with a ~60-residue DNA-binding domain containing a highly conserved heptapeptide motif WRKYGQK
References
Aerts JM, Hollak CE (1997) Plasma and metabolic abnormalities in Gaucher’s disease. Bailliere’s clinical haematology. 10(4):691–709
Akamatsu A, Wong HL, Fujiwara M, Okuda J, Nishide K, Uno K, Imai K, Umemura K, Kawasaki T, Kawano Y et al (2013) An OsCEBiP/OsCERK1-OsRacGEF1-OsRac1 module is an essential early component of chitin-induced rice immunity. Cell Host Microbe 13(4):465–476. https://doi.org/10.1016/j.chom.2013.03.007
Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Moestrup SK, Holmskov U (2009) Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin. J Immunol 183:3800–3809
Becker KL, Aimanianda V, Wang X, Gresnigt MS, Ammerdorffer A, Jacobs CW, Gazendam RP, Joosten LAB, Netea MG, Latge JP et al (2016) Aspergillus cell wall chitin induces anti- and proinflammatory cytokines in Human PBMCs via the Fc-gamma Receptor/Syk/PI3 K Pathway. Mbio 7(3). https://doi.org/10.1128/mBio:01823-15
Boot RG, Blommaart EF, Swart E, Ghauharali-van der Vlugt K, Bijl N, Moe C, Place A, Aerts JM (2001) Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. J Biol Chem 276(9):6770–6778. https://doi.org/10.1074/jbc.M009886200
Boot RG, Renkema GH, Strijland A, van Zonneveld AJ, Aerts JM (1995) Cloning of a cDNA encoding chitotriosidase, a human chitinase produced by macrophages. J Biol Chem 270(44):26252–26256
Bourgeois C, Majer O, Frohner IE, Lesiak-Markowicz I, Hildering K-S, Glaser W, Stockinger S, Decker T, Akira S, Mueller M et al (2011) Conventional dendritic cells mount a Type I IFN response against Candida spp. requiring novel phagosomal TLR7-mediated IFN-beta signaling. J Immunol 186(5):3104–3112. https://doi.org/10.4049/jimmunol.1002599
Bowman SM, Free SJ (2006) The structure and synthesis of the fungal cell wall. BioEssays 28(8):799–808. https://doi.org/10.1002/bies.20441
Bozsoki Z, Cheng J, Feng F, Gysel K, Vinther M, Andersen KR, Oldroyd G, Blaise M, Radutoiu S, Stougaard J (2017) Receptor-mediated chitin perception in legume roots is functionally separable from Nod factor perception. Proc Natl Acad Sci USA 114(38):E8118–E8127. https://doi.org/10.1073/pnas.1706795114
Brown GD, Denning DW, Gow NAR, Levitz SM, Netea MG, White TC (2012) Hidden killers: human fungal infections. Sci Transl Med 4(165). https://doi.org/10.1126/scitranslmed.3004404
Bryant CE, Orr S, Ferguson B, Symmons MF, Boyle JP, Monie TP (2015) International Union of Basic and Clinical Pharmacology. XCVI. Pattern recognition receptors in health and disease. Pharmacol Rev 67(2):462–504. https://doi.org/10.1124/pr.114.009928
Bussink AP, Vreede J, Aerts JM, Boot RG (2008) A single histidine residue modulates enzymatic activity in acidic mammalian chitinase. FEBS Lett 582(6):931–935. https://doi.org/10.1016/j.febslet.2008.02.032
Cao Y, Liang Y, Tanaka K, Nguyen CT, Jedrzejczak RP, Joachimiak A, Stacey G (2014) The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1. Elife. 3. https://doi.org/10.7554/elife.03766
Carotenuto G, Chabaud M, Miyata K, Capozzi M, Takeda N, Kaku H, Shibuya N, Nakagawa T, Barker DG, Genre A (2017) The rice LysM receptor-like kinase OsCERK1 is required for the perception of short-chain chitin oligomers in arbuscular mycorrhizal signaling. New Phytol 214(4):1440–1446. https://doi.org/10.1111/nph.14539
Cash HL, Whitham CV, Behrendt CL, Hooper LV (2006) Symbiotic Bacteria direct expression of an intestinal bactericidal lectin. Science 313(5790):1126–1130
Chelsea L, Bueter CAS, Stuart M, Levitz (2013) Innate sensing of chitin and chitosan. PLoS Pathog 9(1):e1003080
Cuesta A, Esteban MÁ, Meseguer J (2003) In vitro effect of chitin particles on the innate cellular immune system of gilthead seabream (Sparus aurata L.). Fish Shellfish Immunol 15(1):1–11
Da Silva CA, Chalouni C, Williams A, Hartl D, Lee CG, Elias JA (2009) Chitin is a size-dependent regulator of macrophage TNF and IL-10 production. J Immunol 182(6):3573–3582. https://doi.org/10.4049/jimmunol.0802113
Da Silva CA, Hartl D, Liu W, Lee CG, Elias JA (2008) TLR-2 and IL-17A in chitin-induced macrophage activation and acute inflammation. J Immunol 181(6):4279–4286. https://doi.org/10.4049/jimmunol.181.6.4279
Di Rosa M, Distefano G, Zorena K, Malaguarnera L (2016) Chitinases and immunity: ancestral molecules with new functions. Immunobiol 221(3):399–411. https://doi.org/10.1016/j.imbio.2015.11.014
Dodds PN, Rathjen JP (2010) Plant immunity: towards an integrated view of plant-pathogen interactions. Nat Rev Genet 11(8):539–548. https://doi.org/10.1038/nrg2812
Dong B, Li D, Li R, Chen SC-A, Liu W, Liu W, Chen L, Chen Y, Zhang X, Tong Z (2014) A chitin-like component on sclerotic cells of Fonsecaea pedrosoi inhibits dectin-1-mediated murine Th17 development by masking β-glucans. PLoS ONE 9(12):e114113
Dostert C, Tschopp J (2007) DEteCTINg fungal pathogens. Nat Immunol 8(1):17
Elias JA (2004) Acidic mammalian chitinase in Asthmatic Th2 inflammation and IL-13 pathway activation. Science 304:1678–1682
Erwig J, Ghareeb H, Kopischke M, Hacke R, Matei A, Petutschnig E, Lipka V (2017) Chitin-induced and chitin elicitor receptor kinase1 (CERK1) phosphorylation-dependent endocytosis of Arabidopsis thaliana lysin motif-containing receptor-like kinase5 (LYK5). New Phytol 215(1):382–396. https://doi.org/10.1111/nph.14592
Faulkner C, Petutschnig E, Benitez-Alfonso Y, Beck M, Robatzek S, Lipka V, Maule AJ (2013) LYM2-dependent chitin perception limits molecular flux via plasmodesmata. Proc Natl Acad Sci USA 110(22):9166–9170. https://doi.org/10.1073/pnas.1203458110
Felix G, Duran JD, Volko S, Boller T (1999) Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. Plant J 18(3):265–276. https://doi.org/10.1046/j.1365-313X.1999.00265.x
Fernandes C, Gow NAR, Goncalves T (2016) The importance of subclasses of chitin synthase enzymes with myosin-like domains for the fitness of fungi. Fungal Biol Rev 30(1):1–14. https://doi.org/10.1016/j.fbr.2016.03.002
Fuchs K, Cardona Gloria Y, Wolz O-O, Herster F, Sharma L, Dillen CA, Taumer C, Dickhofer S, Bittner Z, Dang T-M et al (2018) The fungal ligand chitin directly binds TLR2 and triggers inflammation dependent on oligomer size. EMBO reports 19(12). https://doi.org/10.15252/embr.201846065
Gimenez-Ibanez S, Hann DR, Ntoukakls V, Petutschnig E, Lipka V, Rathjen JP (2009) AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants. Curr Biol 19(5):423–429. https://doi.org/10.1016/j.cub.2009.01.054
Giorda R, Rudert WA, Vavassori C, Chambers WH, Hiserodt JC, Trucco M (1990) NKR-P1, a signal transduction molecule on natural killer cells. Science 249(4974):1298–1300
Gow NAR, Latge J-P, Munro CA (2017) The fungal cell wall: structure, biosynthesis, and function. Microbiol Spectr 5(3). https://doi.org/10.1128/microbiolspec.funk-0035-2016
Hayafune M, Berisio R, Marchetti R, Silipo A, Kayama M, Desaki Y, Arima S, Squeglia F, Ruggiero A, Tokuyasu K et al (2014) Chitin-induced activation of immune signaling by the rice receptor CEBiP relies on a unique sandwich-type dimerization. Proc Natl Acad Sci USA 111(3):E404–E413. https://doi.org/10.1073/pnas.1312099111
Hollak C, van Weely S, Van Oers M, Aerts J (1994) Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J Clinic Investig 93(3):1288–1292
Kaku H, Nishizawa Y, Ishii-Minami N, Akimoto-Tomiyama C, Dohmae N, Takio K, Minami E, Shibuya N (2006) Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor. Proc Natl Acad Sci USA 103(29):11086–11091. https://doi.org/10.1073/pnas.0508882103
Kanda Y, Yokotani N, Maeda S, Nishizawa Y, Kamakura T, Mori M (2017) The receptor-like cytoplasmic kinase BSR1 mediates chitin-induced defense signaling in rice cells. Biosci Biotech Biochem 81(8):1497–1502
Kim LK, Morita R, Kobayashi Y, Eisenbarth SC, Lee CG, Elias J, Eynon EE, Flavell RA (2015) AMCase is a crucial regulator of type 2 immune responses to inhaled house dust mites. Proc Natl Acad Sci USA 112(22):E2891–2899. https://doi.org/10.1073/pnas.1507393112
Klauser D, Flury P, Boller T, Bartels S (2013) Several MAMPs, including chitin fragments, enhance at Pep-triggered oxidative burst independently of wounding. Plant Signal Behav 8(9):e25346
Koller B, Müller-Wiefel AS, Rupec R, Korting HC, Ruzicka T (2011) Chitin modulates innate immune responses of keratinocytes. PLoS ONE 6(2):e16594
Komi DEA, Sharma L, Dela Cruz CS (2018) Chitin and its effects on inflammatory and immune responses. Clin Rev Allergy Immunol 54(2):213–223. https://doi.org/10.1007/s12016-017-8600-0
Kouzai Y, Mochizuki S, Nakajima K, Desaki Y, Hayafune M, Miyazaki H, Yokotani N, Ozawa K, Minami E, Kaku H et al (2014) Targeted Gene Disruption of OsCERK1 Reveals Its Indispensable Role in Chitin Perception and Involvement in the Peptidoglycan Response and Immunity in Rice. Mol Plant-Microbe Interact 27(9):975–982. https://doi.org/10.1094/mpmi-03-14-0068-r
Kzhyshkowska JG, Goerdt A, Sergij (2007) Human chitinases and chitinase-like proteins as indicators for inflammation and cancer. Biomark Insights 2:117727190700200023
Laluk K, Luo H, Chai M, Dhawan R, Lai Z, Mengiste T (2011) Biochemical and genetic requirements for function of the immune response regulator botrytis-induced kinase1 in plant growth, ethylene signaling, and PAMP-triggered immunity in arabidopsis. Plant Cell 23(8):2831–2849. https://doi.org/10.1105/tpc.111.087122
Latge J-P (2007) The cell wall: a carbohydrate armour for the fungal cell. Molec Microbiol 66(2):279–290. https://doi.org/10.1111/j.1365-2958.2007.05872.x
Le MH, Cao Y, Zhang X-C, Stacey G (2014) LIK1, A CERK1-interacting kinase, regulates plant immune responses in arabidopsis. Plos One 9(7). https://doi.org/10.1371/journal.pone.0102245
Lee CG, Da Silva CA, Dela Cruz CS, Ahangari F, Ma B, Kang M-J, He C-H, Takyar S, Elias JA (2011) Role of chitin and chitinase/chitinase-like proteins in inflammation, tissue remodeling, and injury. Ann Rev Physiol 73:479–501
Lee CG, Da Silva CA, Lee J-Y, Hartl D, Elias JA (2008) Chitin regulation of immune responses: an old molecule with new roles. Curr Opinion Immunol 20(6):684–689
Lee W-S, Rudd JJ, Hammond-Kosack KE, Kanyuka K (2014) Mycosphaerella graminicola LysM effector-mediated stealth pathogenesis subverts recognition through both CERK1 and CEBiP homologues in wheat. Molec Plant-Microbe Interact 27(3):236–243. https://doi.org/10.1094/mpmi-07-13-0201-r
Liu B, Li J-F, Ao Y, Qu J, Li Z, Su J, Zhang Y, Liu J, Feng D, Qi K et al (2012a) Lysin Motif-containing Proteins LYP4 and LYP6 play dual roles in peptidoglycan and chitin perception in rice innate immunity. Plant Cell 24(8):3406–3419. https://doi.org/10.1105/tpc.112.102475
Liu T, Liu Z, Song C, Hu Y, Han Z, She J, Fan F, Wang J, Jin C, Chang J et al (2012b) Chitin-induced dimerization activates a plant immune receptor. Science 336(6085):1160–1164. https://doi.org/10.1126/science.1218867
Liu S, Wang J, Han Z, Gong X, Zhang H, Chai J (2016) Molecular mechanism for fungal cell wall recognition by rice chitin receptor OsCEBiP. Structure 24(7):1192–1200. https://doi.org/10.1016/j.str.2016.04.014
Luna E, Pastor V, Robert J, Flors V, Mauch-Mani B, Ton J (2011) Callose deposition: a multifaceted plant defense response. Molec Plant-Microbe Interact 24(2):183–193. https://doi.org/10.1094/mpmi-07-10-0149
Lund S, Walford HH, Doherty TA (2013). Type 2 innate lymphoid cells in allergic disease. Curr Immunol Rev 9(4):214-221
Mack I, Hector A, Ballbach M, Kohlhaufl J, Fuchs KJ, Weber A, Mall MA, Hartl D (2015) The role of chitin, chitinases, and chitinase-like proteins in pediatric lung diseases. Molec Cell Pediatr 2(1):3–3. https://doi.org/10.1186/s40348-015-0014-6
Malaguarnera L (2006) Chitotriosidase: the yin and yang. Cell Mol Life Sci CMLS 63(24):3018–3029
Malaguarnera L, Di Rosa M, Zambito AM, dell’Ombra N, Nicoletti F, Malaguarnera M (2006) Chitotriosidase gene expression in Kupffer cells from patients with non-alcoholic fatty liver disease. Gut 55(9):1313–1320
Medzhitov R (2007) Recognition of microorganisms and activation of the immune response. Nature 449(7164):819–826. https://doi.org/10.1038/nature06246
Miya A, Albert P, Shinya T, Desaki Y, Ichimura K, Shirasu K, Narusaka Y, Kawakami N, Kaku H, Shibuya N (2007) CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis. Proc Natl Acad Sci USA 104(49):19613–19618. https://doi.org/10.1073/pnas.0705147104
Nair MG, Gallagher IJ, Taylor MD, Loke Pn, Coulson PS, Wilson R, Maizels RM, Allen JE (2005) Chitinase and Fizz family members are a generalized feature of nematode infection with selective upregulation of Ym1 and Fizz1 by antigen-presenting cells. Infect Immun 73(1):385–394
Olland AM, Strand J, Presman E, Czerwinski R, Joseph-McCarthy D, Krykbaev R, Schlingmann G, Chopra R, Lin L, Fleming M et al (2009) Triad of polar residues implicated in pH specificity of acidic mammalian chitinase. Protein Sci: Publ Protein Soc 18(3):569–578. https://doi.org/10.1002/pro.63
Petutschnig EK, Jones AME, Serazetdinova L, Lipka U, Lipka V (2010) The lysin motif receptor-like kinase (LysM-RLK) CERK1 is a major chitin-binding protein in arabidopsis thaliana and subject to chitin-induced phosphorylation. J Biol Chem 285(37):28902–28911. https://doi.org/10.1074/jbc.M110.116657
Reese TA, Liang H-E, Tager AM, Luster AD, Van Rooijen N, Voehringer D, Locksley RM (2007) Chitin induces accumulation in tissue of innate immune cells associated with allergy. Nature 447(7140):92
Roy RM, Wüthrich M, Klein BS (2012) Chitin elicits CCL2 from airway epithelial cells and induces CCR62-dependent innate allergic inflammation in the lung. J Immunol 189(5):2545–2552
Sanchez-Vallet A, Mesters JR, Thomma BPHJ (2015) The battle for chitin recognition in plant-microbe interactions. FEMS Microbiol Rev 39(2):171–183. https://doi.org/10.1093/femsre/fuu003
Satoh T, Takeuchi O, Vandenbon A, Yasuda K, Tanaka Y, Kumagai Y, Miyake T, Matsushita K, Okazaki T, Saitoh T (2010) The Jmjd3-Irf4 axis regulates M2 macrophage polarization and host responses against helminth infection. Nat Immunol 11(10):936
Schlosser A, Thomsen T, Moeller JB, Nielsen O, Tornøe I, Mollenhauer J, Moestrup SK, Holmskov U (2009) Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin. J Immunol 183(6):3800–3809
Semeňuk T, Krist P, Pavlíček J, Bezouška K, Kuzma M, Novák P, Křen V (2001) Synthesis of chitooligomer-based glycoconjugates and their binding to the rat natural killer cell activation receptor NKR-P1. Glycoconj J 18(10):817–826
Shen C-R, Juang H-H, Chen H-S, Yang C-J, Wu C-J, Lee M-H, Hwang Y-S, Kuo M-L, Chen Y-S, Chen J-K et al (2015) The correlation between chitin and acidic mammalian chitinase in animal models of allergic asthma. Int J Mol Sci 16(11):27371–27377. https://doi.org/10.3390/ijms161126033
Shibata Y, Foster LA, Bradfield JF, Myrvik QN (2000) Oral administration of chitin down-regulates serum IgE levels and lung eosinophilia in the allergic mouse. J Immunol 164(3):1314–1321
Shibata Y, Metzger WJ, Myrvik QN (1997) Chitin particle-induced cell-mediated immunity is inhibited by soluble mannan - Mannose receptor-mediated phagocytosis initiates IL-12 production. J Immunol 159(5):2462–2467
Shimizu T, Nakano T, Takamizawa D, Desaki Y, Ishii-Minami N, Nishizawa Y, Minami E, Okada K, Yamane H, Kaku H et al (2010) Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signaling in rice. Plant J 64(2):204–214. https://doi.org/10.1111/j.1365-313X.2010.04324.x
Shinya T, Motoyama N, Ikeda A, Wada M, Kamiya K, Hayafune M, Kaku H, Shibuya N (2012) Functional characterization of CEBiP and CERK1 homologs in arabidopsis and rice reveals the presence of different chitin receptor systems in plants. Plant Cell Physiol 53(10):1696–1706. https://doi.org/10.1093/pcp/pcs113
Shinya T, Nakagawa T, Kaku H, Shibuya N (2015) Chitin-mediated plant-fungal interactions: catching, hiding and handshaking. Curr Opin Plant Biol 26:64–71. https://doi.org/10.1016/j.pbi.2015.05.032
Shinya T, Yamaguchi K, Desaki Y, Yamada K, Narisawa T, Kobayashi Y, Maeda K, Suzuki M, Tanimoto T, Takeda J et al (2014) Selective regulation of the chitin-induced defense response by the Arabidopsis receptor-like cytoplasmic kinase PBL27. Plant J 79(1):56–66. https://doi.org/10.1111/tpj.12535
Shuhui L, Mok Y-K, Wong WSF (2009) Role of mammalian chitinases in asthma. Int Arch Allergy Immunol 149(4):369–377. https://doi.org/10.1159/000205583
Spoel SH, Dong X (2012) How do plants achieve immunity? Defence without specialized immune cells. Nat Rev Immunol 12(2):89–100. https://doi.org/10.1038/nri3141
Tada R, Latge J-P, Aimanianda V (2013) Undressing the fungal cell wall/cell membrane - the antifungal drug targets. Curr Pharm Design 19(20):3738–3747. https://doi.org/10.2174/1381612811319200012
Thomsen T, Schlosser A, Holmskov U, Sorensen GL (2011) Ficolins and FIBCD1: soluble and membrane bound pattern recognition molecules with acetyl group selectivity. Mol Immunol 48(4):369–381
Tomas Semenuk PK, Pavlıcek Jirı, Bezouska Karel, Kuzma Marek, Novak Petr, Kren Vladimır (2001) Synthesis of chitooligomer-based glycoconjugates and their binding to the rat natural killer cell activation receptor NKR-P1. Glycoconj J 18:817–826
Tschopp CDJ (2007) DEteCTINg fungal pathogens. J Biol Chem 8:17–18. https://doi.org/10.1074/jbc
van der Luit AH, Piatti T, van Doorn A, Musgrave A, Felix G, Boller T, Munnik T (2000) Elicitation of suspension-cultured tomato cells triggers the formation of phosphatidic acid and diacylglycerol pyrophosphate. Plant Physiol 123(4):1507–1515. https://doi.org/10.1104/pp.123.4.1507
Van Dyken SJ, Mohapatra A, Nussbaum JC, Molofsky AB, Thornton EE, Ziegler SF, McKenzie AN, Krummel MF, Liang H-E, Locksley RM (2014) Chitin activates parallel immune modules that direct distinct inflammatory responses via innate lymphoid type 2 and γδ T cells. Immunity 40(3):414–424
Vannella KM, Ramalingam TR, Hart KM, de Queiroz Prado R, Sciurba J, Barron L, Borthwick LA, Smith AD, Mentink-Kane M, White S et al (2016) Acidic chitinase primes the protective immune response to gastrointestinal nematodes. Nat Immunol 17(5):538–544. https://doi.org/10.1038/ni.3417
Wagener J, Malireddi RS, Lenardon MD, Köberle M, Vautier S, MacCallum DM, Biedermann T, Schaller M, Netea MG, Kanneganti T-D (2014) Fungal chitin dampens inflammation through IL-10 induction mediated by NOD2 and TLR9 activation. PLoS Pathog 10(4):e1004050
Wan J, Zhang X-C, Neece D, Ramonell KM, Clough S, Kim S-Y, Stacey MG, Stacey G (2008) A LysM receptor-like kinase plays a critical role in chitin signaling and fungal resistance in Arabidopsis. Plant Cell 20(2):471–481. https://doi.org/10.1105/tpc.107.056754
Wan JR, Zhang SQ, Stacey G (2004) Activation of a mitogen-activated protein kinase pathway in Arabidopsis by chitin. Mol Plant Pathol 5(2):125–135. https://doi.org/10.1111/j.1364-3703.2004.00215.x
Wiesner DL, Specht CA, Lee CK, Smith KD, Mukaremera L, Lee ST, Lee CG, Elias JA, Nielsen JN, Boulware DR (2015) Chitin recognition via chitotriosidase promotes pathologic type-2 helper T cell responses to cryptococcal infection. PLoS Pathog 11(3):e1004701
Yamaguchi K, Imai K, Akamatsu A, Mihashi M, Hayashi N, Shimamoto K, Kawasaki T (2012) SWAP70 functions as a Rac/Rop guanine nucleotide-exchange factor in rice. Plant J 70(3):389–397. https://doi.org/10.1111/j.1365-313X.2011.04874.x
Yamaguchi K, Yamada K, Ishikawa K, Yoshimura S, Hayashi N, Uchihashi K, Ishihama N, Kishi-Kaboshi M, Takahashi A, Tsuge S et al (2013) A receptor-like cytoplasmic kinase targeted by a plant pathogen effector is directly phosphorylated by the chitin receptor and mediates rice immunity. Cell Host Microbe 13(3):347–357. https://doi.org/10.1016/j.chom.2013.02.007
Yeh Y-H, Panzeri D, Kadota Y, Huang Y-C, Huang P-Y, Tao C-N, Roux M, Chien H-C, Chin T-C, Chu P-W et al (2016) The Arabidopsis Malectin-like/LRR-RLK IOS1 is critical for BAK1-dependent and BAK1-independent pattern-triggered immunity. Plant Cell 28(7):1701–1721. https://doi.org/10.1105/tpc.16.00313
Zhang J, Li W, Xiang T, Liu Z, Laluk K, Ding X, Zou Y, Gao M, Zhang X, Chen S et al (2010) Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a pseudomonas syringae effector. Cell Host Microbe 7(4):290–301. https://doi.org/10.1016/j.chom.2010.03.007
Zipfel C, Oldroyd GED (2017) Plant signalling in symbiosis and immunity. Nature 543(7645):328–336. https://doi.org/10.1038/nature22009
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Jiang, X., Bao, H., Merzendorfer, H., Yang, Q. (2019). Immune Responses of Mammals and Plants to Chitin-Containing Pathogens. In: Yang, Q., Fukamizo, T. (eds) Targeting Chitin-containing Organisms. Advances in Experimental Medicine and Biology, vol 1142. Springer, Singapore. https://doi.org/10.1007/978-981-13-7318-3_4
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