Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Host organism: Arabidopsis thaliana
NCBI PubMed ID: 29083116Publication DOI: 10.1111/tpj.13755Journal NLM ID: 2985193RPublisher: Columbus, OH: American Chemical Society
Correspondence: Molina A <antonio.molina
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Institutions: Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid (UPM) - Instituto Nacional de Investigación y Tecnología Agraria y Alimentaria (INIA), Campus de Montegancedo UPM, Madrid, Spain, Departamento de Biotecnología-Biología Vegetal, Escuela Técnica Superior de Ingeniería Agronómica, Alimentaría y de Biosistemas, UPM, Madrid, Spain, Departamento de Sistemas y Recursos Naturales, Escuela Técnica Superior de Ingeniería de Montes, UPM, Madrid, Spain
Fungal cell walls, which are essential for environmental adaptation and host colonization by the fungus, have been evolutionarily selected by plants and animals as a source of microbe-associated molecular patterns (MAMPs) that, upon recognition by host pattern recognition receptors (PRRs), trigger immune responses conferring disease resistance. Chito-oligosaccharides [β-1,4-N-acetylglucosamine oligomers, (GlcNAc)n ] are the only glycosidic structures from fungal walls that have been well-demonstrated to function as MAMPs in plants. Perception of (GlcNAc)4-8 by Arabidopsis involves CERK1, LYK4 and LYK5, three of the eight members of the LysM PRR family. We found that a glucan-enriched wall fraction from the pathogenic fungus Plectosphaerella cucumerina which was devoid of GlcNAc activated immune responses in Arabidopsis wild-type plants but not in the cerk1 mutant. Using this differential response, we identified the non-branched 1,3-β-D-(Glc) hexasaccharide as a major fungal MAMP. Recognition of 1,3-β-D-(Glc)6 was impaired in cerk1 but not in mutants defective in either each of the LysM PRR family members or in the PRR-co-receptor BAK1. Transcriptomic analyses of Arabidopsis plants treated with 1,3-β-D-(Glc)6 further demonstrated that this fungal MAMP triggers the expression of immunity-associated genes. In silico docking analyses with molecular mechanics and solvation energy calculations corroborated that CERK1 can bind 1,3-β-D-(Glc)6 at effective concentrations similar to those of (GlcNAc)4 . These data support that plants, like animals, have selected as MAMPs the linear 1,3-β-D-glucans present in the walls of fungi and oomycetes. Our data also suggest that CERK1 functions as an immune co-receptor for linear 1,3-β-D-glucans in a similar way to its proposed function in the recognition of fungal chito-oligosaccharides and bacterial peptidoglycan MAMPs.
cell wall, glucan, Plant immunity, chitin, CERK, BAK1, necrotrophic fungi
Structure type: structural motif or average structure
Location inside paper: Abstract
Trivial name: chitin
Compound class: cell wall polysaccharide, glucan, cell wall polisaccharide
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_153212,IEDB_241099,IEDB_423114,IEDB_423150,SB_74,SB_85
Methods: methylation, acid hydrolysis, GC, biological assays, extraction, MALDI-TOF, TFA hydrolysis
Biological activity: functions as MAMP; binds with LysM PRR family members AtLYK4, AtLYK5; activates Arabidopsis PTI responses(cytoplasmic Ca2+ influxes, MAPKs phosphorylation and up-regulation of PTI marker genes)
Related record ID(s): 48634, 48636, 48650, 48651, 48652, 48689, 48691, 48694, 48715, 48752, 48757, 48764, 48769, 48785, 48794, 48795, 48801, 48804, 48828, 48853, 48872, 48900, 48901, 48902, 48984
NCBI Taxonomy refs (TaxIDs): 40658Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
There is only one chemically distinct structure:
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