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The role of chitin detection in plant–pathogen interactions
Open accessAbstract
Despite the deployment of antifungal defence strategies, fungal diseases occur in all types of multicellular organisms. In plants, the role of fungal chitin as pathogen-associated molecular pattern that activates host defence is well established. Interestingly, plants employ homologs of the chitin immune receptors to initiate microbial symbiosis. Accumulating evidence shows that fungal pathogens developed secreted effectors to disarm chitin-triggered host immunity.
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Chitinases likely also affect biocontrol activity indirectly because chito-oligosaccharides are potent inducers of plant immune responses.
“Chitinases likely also affect biocontrol activity indirectly, because chito-oligosaccharides (CHOS; the results of chitin degradation) are potent inducers of plant immune responses (Kombrink et al. 2011; Langner and Gohre 2015; Liu et al. 2012, 2014).”
From Biocontrol yeasts: mechanisms and applications (2019) · cites this paper as Kombrink et al. 2011
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Lipo-chitooligosaccharide Signaling in Endosymbiotic Plant-Microbe Interactions
Gough, C., & Cullimore, J. (2011) · Molecular Plant-Microbe Interactions® · doi:10.1094/mpmi-01-11-0019 · Cited by 254
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Research works printed but not linked: 82
- Bowman, 2006, The structure and synthesis of the fungal cell wall, Bioessays, 28, 799, 10.1002/bies.20441 · DOI
- Lenardon, 2010, Chitin synthesis and fungal pathogenesis, Curr. Opin. Microbiol., 13, 416, 10.1016/j.mib.2010.05.002 · DOI · Paper page
- Latgé, 2007, The cell wall: a carbohydrate armour for the fungal cell, Mol. Microbiol., 66, 279, 10.1111/j.1365-2958.2007.05872.x · DOI · Paper page
- Latgé, 2010, Tasting the fungal cell wall, Cell. Microbiol., 12, 863, 10.1111/j.1462-5822.2010.01474.x · DOI
- Boller, 2009, A renaissance of elicitors: perception of microbe-associated molecular patterns and danger signals by pattern recognition receptors, Annu. Rev. Plant Biol., 60, 379, 10.1146/annurev.arplant.57.032905.105346 · DOI
- Felix, 1993, Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: induction of extracellular alkalinization, changes in protein phosphorylation, and establishment of a refractory state, Plant J., 4, 307, 10.1046/j.1365-313X.1993.04020307.x · DOI
- Shibuya, 1993, Identification of a novel high-affinity binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction from suspension-cultured rice cells, FEBS Lett., 329, 75, 10.1016/0014-5793(93)80197-3 · DOI
- Osbourn, 1996, Preformed antimicrobial compounds and plant defence against fungal attack, Plant Cell, 8, 1821, 10.2307/3870232 · DOI
- Broekaert, 1997, Antimicrobial peptides from plants, Crit. Rev. Plant Sci., 16, 297, 10.1080/07352689709701952 · DOI
- Dixon, 1994, Early events in the activation of plant defence responses, Annu. Rev. Phytopathol., 32, 479, 10.1146/annurev.py.32.090194.002403 · DOI
- Thomma, 2001, The complexity of disease signalling in Arabidopsis, Curr. Opin. Immunol., 13, 63, 10.1016/S0952-7915(00)00183-7 · DOI
- Ryals, 1996, Systemic acquired resistance, Plant Cell, 8, 1809, 10.2307/3870231 · DOI
- Thomma, 2011, Of PAMPs and effectors: the blurred PTI-ETI dichotomy, Plant Cell, 23, 4, 10.1105/tpc.110.082602 · DOI
- Jones, 2006, The plant immune system, Nature, 444, 323, 10.1038/nature05286 · DOI · Paper page
- Panstruga, 2009, Terrific protein traffic: the mystery of effector protein delivery by filamentous plant pathogens, Science, 8, 748, 10.1126/science.1171652 · DOI
- de Jonge, 2011, How filamentous pathogens co-opt plants: the ins and outs of fungal effectors, Curr. Opin. Plant Biol., 14, 1, 10.1016/j.pbi.2011.03.005 · DOI
- Shan, 2008, Bacterial effectors target the common signalling partner BAK1 to disrupt multiple MAMP receptor-signalling complexes and impede plant immunity, Cell Host Microbe., 4, 17, 10.1016/j.chom.2008.05.017 · DOI
- Gimenez-Ibanez, 2009, AvrPtoB targets the LysM receptor kinase CERK1 to promote bacterial virulence on plants, Curr. Biol., 19, 423, 10.1016/j.cub.2009.01.054 · DOI
- Joosten, 1994, Host resistance to a fungal tomato pathogen lost by a single base pair change in an avirulence gene, Nature, 367, 384, 10.1038/367384a0 · DOI
- Houterman, 2008, Suppression of plant resistance gene-based immunity by a fungal effector, PLoS Pathog., 4, 1, 10.1371/journal.ppat.1000061 · DOI
- Schlumbaum, 1986, Plant chitinases are potent inhibitors of fungal growth, Nature, 324, 365, 10.1038/324365a0 · DOI
- Grison, 1996, Field tolerance to fungal pathogens of Brassica napus constitutively expressing a chimeric chitinase gene, Nat. Biotechnol., 14, 643, 10.1038/nbt0596-643 · DOI
- Nishizawa, 1999, Regulation of the chitinase gene expression in suspension-cultured rice cells by N-acetylchitooligochsaccharides: differences in the signal transduction pathways leading to the activation of elicitor-responsive genes, Plant Mol. Biol., 39, 907, 10.1023/A:1006161802334 · DOI
- Ito, 1997, Identification of a high-affinity binding protein for N-acetylchitooligosaccharide elicitor in the plasma membrane of suspension-cultured rice cells by affinity labeling, Plant J., 12, 347, 10.1046/j.1365-313X.1997.12020347.x · DOI
- Kaku, 2006, Plant cells recognize chitin fragments for defence signalling through a plasma membrane receptor, Proc. Natl. Acad. Sci. U.S.A., 103, 11086, 10.1073/pnas.0508882103 · DOI
- Kishimoto, 2010, Perception of the chitin oligosaccharide contributes to disease resistance to blast fungus Magnaporthe oryzae in rice, Plant J., 64, 343, 10.1111/j.1365-313X.2010.04328.x · DOI
- Shimizu, 2010, Two LysM receptor molecules, CEBiP and OsCERK1, cooperatively regulate chitin elicitor signalling in rice, Plant J., 64, 204, 10.1111/j.1365-313X.2010.04324.x · DOI
- Miya, 2007, CERK1, a LysM receptor kinase, is essential for chitin elicitor signalling in Arabidopsis, Proc. Natl. Acad. Sci. U.S.A., 104, 19613, 10.1073/pnas.0705147104 · DOI
- Wan, 2008, A LysM receptor-like kinase plays a critical role in chitin signalling and fungal resistance in Arabidopsis, Plant Cell, 20, 471, 10.1105/tpc.107.056754 · DOI
- Petutschnig, 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, 28902, 10.1074/jbc.M110.116657 · DOI
- Iizasa, 2010, Direct binding of a plant receptor-like kinase, LysM RLK1/CERK1, to chitin in vitro, J. Biol. Chem., 285, 2996, 10.1074/jbc.M109.027540 · DOI
- Tanaka, 2010, HvCEBiP, a gene homologues to rice chitin receptor CEBiP, contributes to basal resistance of barley to Magnaporthe oryzae, BMC Plant Biol., 10, 228, 10.1186/1471-2229-10-288 · DOI
- Fliegmann, 2011, Biochemical and phylogenetic analysis of CEBiP-like LysM domain-containing extracellular proteins in higher plants, Plant Phys. Biochem., 49, 709, 10.1016/j.plaphy.2011.04.004 · DOI
- Garvey, 1986, Nucleotide sequence of Bacillus phage Ø29 genes 14 and 15 with other phage lysozymes, Nucl. Acids Res., 14, 100001, 10.1093/nar/14.24.10001 · DOI
- Eckert, 2006, Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis, J. Bacteriol., 188, 8513, 10.1128/JB.01145-06 · DOI
- Buist, 2008, LysM, a widely distributed protein motif for binding to (peptido)glycans, Mol. Microbiol., 68, 838, 10.1111/j.1365-2958.2008.06211.x · DOI
- Bateman, 2000, The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD), J. Mol. Biol., 299, 1113, 10.1006/jmbi.2000.3778 · DOI · Paper page
- Ohnuma, 2008, LysM domains from Pteris ryukyuensis chitinase-A, J. Biol. Chem., 283, 5178, 10.1074/jbc.M707156200 · DOI
- Koharudin, 2011, Structure–function analysis of a CVNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe Oryzae, Structure, 19, 662, 10.1016/j.str.2011.03.004 · DOI
- Thomma, 2005, Cladosporium fulvum (syn. Passalora fulva), a highly specialized plant pathogen as a model for functional studies on plant pathogenic Mycosphaerellaceae, Mol, Plant Pathol., 6, 379
- Joosten, 1999, The tomato-Cladosporium fulvum interaction: a versatile experimental system to study plant-pathogen interactions, Annu. Rev. Phytopathol., 37, 335, 10.1146/annurev.phyto.37.1.335 · DOI
- Westerink, 2002, The Avr4 elicitor protein of Cladosporium fulvum binds to fungal components with high affinity, Mol. Plant Microbe Interact., 15, 1219, 10.1094/MPMI.2002.15.12.1219 · DOI
- van den Burg, 2003, Natural disulfide bond-disrupted mutants of Avr4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4 mediated resistance, but retain their chitin binding ability, J. Biol. Chem., 278, 27340, 10.1074/jbc.M212196200 · DOI
- van den Burg, 2004, Binding of the Avr4 elicitor of Cladosporium fulvum to chitotriose units is facilitated by positive allosteric protein–protein interactions, J. Biol. Chem., 279, 16786, 10.1074/jbc.M312594200 · DOI
- Van den Burg, 2006, Cladosporium fulvum Avr4 protects fungal cell wall against hydrolysis by plant chitinases accumulating during infection, Mol. Plant Microbe Interact., 19, 1420, 10.1094/MPMI-19-1420 · DOI
- van Esse, 2007, The chitin-binding Cladosporium fulvum effector protein Avr4 is a virulence factor, Mol. Plant Microbe Interact., 20, 1092, 10.1094/MPMI-20-9-1092 · DOI
- Bolton, 2008, The novel Cladosporium fulvum lysin motif effector Ecp6 is a virulence factor with orthologues in other fungal species, Mol. Microbiol., 69, 119, 10.1111/j.1365-2958.2008.06270.x · DOI
- de Jonge, 2010, Conserved fungal LysM effector Ecp6 prevents chitin-triggered immunity in plants, Science, 329, 953, 10.1126/science.1190859 · DOI
- Stergiopoulos, 2010, Tomato Cf resistance proteins mediate recognition of cognate homologous effectors from fungi pathogenic on dicots and monocots, Proc. Natl. Acad. Sci. U.S.A., 107, 7610, 10.1073/pnas.1002910107 · DOI
- de Jonge, 2009, Fungal LysM effectors – extinguishers of host immunity?, Trends Microbiol., 17, 151, 10.1016/j.tim.2009.01.002 · DOI
- Marshall, 2011, Analysis of two in planta expressed LysM effector homologues from the fungus Mycosphaerella graminicola reveals novel functional properties and varying contributions to virulence on wheat, Plant Physiol., 156, 756, 10.1104/pp.111.176347 · DOI
- Knogge, 2006, LysM receptors recognize friend and foe, Proc. Natl. Acad. Sci. U.S.A., 103, 10829, 10.1073/pnas.0604601103 · DOI
- Masson-Boivin, 2009, Establishing nitrogen-fixing symbiosis with legumes: how many rhizobium recipes?, Trends Microbiol., 17, 458, 10.1016/j.tim.2009.07.004 · DOI
- Sprent, 2007, Legume evolution, where do nodules and mycorrhizas fit in?, Plant Physiol., 144, 575, 10.1104/pp.107.096156 · DOI
- Oláh, 2005, Nod factors and a diffusible factor from arbuscular mycorrhizal fungi stimulate lateral root formation in Medicago truncatula via the DMI1/DMI2 signalling pathway, Plant J., 44, 195, 10.1111/j.1365-313X.2005.02522.x · DOI
- Parniske, 2008, Arbuscular mycorrhiza: the mother of plant root endosymbioses, Nat. Rev. Microbiol., 6, 763, 10.1038/nrmicro1987 · DOI
- Hamel, 2010, Chitooligosaccharide sensing and downstream signalling: contrasted outcomes in pathogenic and beneficial plant-microbe interactions, Planta, 232, 787, 10.1007/s00425-010-1215-9 · DOI
- Moulin, 2001, Nodulation of legumes by members of the β-subclass of proteobacteria, Nature, 411, 948, 10.1038/35082070 · DOI
- Maillet, 2011, Fungal lipochitooligosaccharide symbiotic signals in arbuscular mycorrhiza, Nature, 469, 58, 10.1038/nature09622 · DOI
- Limpens, 2003, LysM domain receptor kinases regulating rhizobial Nod-factor induced infection, Science, 302, 630, 10.1126/science.1090074 · DOI
- Madsen, 2003, A receptor kinase gene of the LysM type is involved in legume perception of rhizobial signals, Nature, 425, 637, 10.1038/nature02045 · DOI
- Radutoiu, 2003, Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases, Nature, 425, 585, 10.1038/nature02039 · DOI
- Mulder, 2006, LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors, Glycobiology, 16, 801, 10.1093/glycob/cwl006 · DOI
- Radutoiu, 2007, LysM domains mediate lipochitin-oligosaccharides recognition and NfrI genes extend the symbiotic host range, EMBO J., 26, 3923, 10.1038/sj.emboj.7601826 · DOI
- Op den Camp, 2011, LysM-type mycorrhizal receptor recruited for rhizobium symbiosis in nonlegume Parasponia, Science, 331, 909, 10.1126/science.1198181 · DOI
- Zhang, 2007, Molecular evolution of Lysin motif-type receptor-like kinases in plants, Plant Physiol., 144, 623, 10.1104/pp.107.097097 · DOI
- Lohman, 2010, Evolution and regulation of the Lotus japonicus LysM receptor gene family, Mol. Plant Microbe Interact., 23, 510, 10.1094/MPMI-23-4-0510 · DOI
- Nakagawa, 2011, From defence to symbiosis: limited alterations in the kinase domain of LysM receptor-like kinases are crucial for evolution of legume-Rhizobium symbiosis, Plant J., 65, 169, 10.1111/j.1365-313X.2010.04411.x · DOI
- Madsen, 2011, Autophosphorylation is essential for the in vivo function of the Lotus Japonicus Nod factor receptor 1 and receptor-mediated signalling in cooperation with Nod factor receptor 5, Plant J., 65, 404, 10.1111/j.1365-313X.2010.04431.x · DOI
- Güimil, 2005, Comparative transcriptomics of rice reveals an ancient pattern of response to microbial colonization, Proc. Natl. Acad. Sci. U.S.A., 102, 8066, 10.1073/pnas.0502999102 · DOI
- Serna-Sanz, 2011, Phosphoproteome analysis of Lotus japonicus roots reveals shared and distinct components of symbiosis and defence, Mol. Plant Microbe Interact., 8, 932, 10.1094/MPMI-09-10-0222 · DOI
- Shibuya, 2001, Oligosaccharide signalling for defence responses in plant, Physiol. Mol. Plant Pathol., 59, 223, 10.1006/pmpp.2001.0364 · DOI
- Yamada, 1993, Induction of phytoalexin formation in suspension-cultured rice cells by N-acetyl-chitooligosaccharides, Biosci. Biotech. Biochem., 57, 405, 10.1271/bbb.57.405 · DOI
- D’Haeze, 2002, Nod factor structures, responses and perception during initiation of nodule development, Glycobiology, 12, 79R, 10.1093/glycob/12.6.79R · DOI
- Shibata, 1997, Alveolar macrophage priming by intravenous administration of chitin particles, polymers of N-acetyl-d-glucosamine, in mice, Infect. Immun., 65, 1734, 10.1128/iai.65.5.1734-1741.1997 · DOI
- Shibata, 1997, Chitin particle-induced cell-mediated immunity is inhibited by soluble mannan: mannose receptor-mediated phagocytosis initiates IL-12 production, J. Immunol., 159, 2462, 10.4049/jimmunol.159.5.2462 · DOI
- Reese, 2007, Chitin induces accumulation in tissue of innate immune cells associated with allergy, Nature, 447, 92, 10.1038/nature05746 · DOI
- Lee, 2008, Chitin regulation of immune responses: an old molecule with new roles, Curr. Opin. Immunol., 20, 684, 10.1016/j.coi.2008.10.002 · DOI
- Da Silva, 2009, Chitin is a size-dependent regulator of macrophage TNF and IL-10 production, J. Immunol., 182, 3573, 10.4049/jimmunol.0802113 · DOI
- Da Silva, 2008, TLR-2 and IL-17A in chitin-induced macrophage activation and acute inflammation, J. Immunol., 181, 4279, 10.4049/jimmunol.181.6.4279 · DOI
- Mora-Montes, 2011, Recognition and blocking of innate immunity cells by Candida albicans chitin, Infect. Immun., 79, 1961, 10.1128/IAI.01282-10 · DOI
- Schlosser, 2009, Characterization of FIBCD1 as an acetyl group-binding receptor that binds chitin, J. Immunol., 183, 3800, 10.4049/jimmunol.0901526 · DOI
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Biocontrol yeasts: mechanisms and applications
Freimoser, F. M., Rueda-Mejia, M. P., Tilocca, B., & Migheli, Q. (2019) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-019-2728-4 · Cited by 462
Metadata
- Authors
- Kombrink, A., Sánchez-Vallet, A., & Thomma, B. P. H. J.
- Affiliations
- Wageningen University & Research (NL)
- Corresponding author
- Thomma, Bart P.H.J.
- ORCID
- Thomma, Bart P.H.J.
- Venue
- Microbes and Infection
- Publisher
- Elsevier BV
- Published
- 2011-12
- Volume
- 13
- Issue
- 14-15
- Pages
- 1168-1176
- ISSN
- 1286-4579 (ISSN-L)
- OpenAlex
- W1985942577
- Cited by
- 121
- References
- 1
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 13 · 2023: 10 · 2022: 13 · 2021: 14 · 2020: 12 · 2019: 7 · 2018: 4 · 2017: 5 · 2016: 6 · 2015: 9 · 2014: 8 · 2013: 7 · 2012: 4
- FWCI
- 0.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Microbes and Infection (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (acceptedVersion, other-oa)
- Socio-Environmental Systems Modeling (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- Universidad Politécnica de Madrid
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Studies on Chitinases and Chitosanases
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Disease Resistance and Genetics
- Keywords
- plant-pathogen interaction, fungal chitin, pathogen-associated molecular patterns, plant immunity, fungal effectors, plant-fungal symbiosis
- MeSH terms
- Chitin, Fungal Proteins, Fungi, Mycoses, Plant Diseases, Plant Proteins, Plants, Rhizobiaceae, Symbiosis, Signal Transduction, Receptors, Pattern Recognition, Host-Pathogen Interactions, Plant Immunity
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