Taxonomic group: fungi / Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Basidiomycota
(Phylum: Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Ascomycota, Basidiomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 30181925Publication DOI: 10.1080/21501203.2018.1473299Journal NLM ID: 101523848Publisher: Abingdon, Oxon: Taylor & Francis
Correspondence: pusztahelyi

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Institutions: Central Laboratory of Agricultural and Food Products, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, Hungary
Chitin is the second abundant polysaccharide in the world after cellulose. It is a vital structural component of the fungal cell wall but not for plants. In plants, fungi are recognised through the perception of conserved microbe-associated molecular patterns (MAMPs) to induce MAMP-triggered immunity (MTI). Chitin polymers and their modified form, chitosan, induce host defence responses in both monocotyledons and dicotyledons. The plants' response to chitin, chitosan, and derived oligosaccharides depends on the acetylation degree of these compounds which indicates possible biocontrol regulation of plant immune system. There has also been a considerable amount of recent research aimed at elucidating the roles of chitin hydrolases in fungi and plants as chitinase production in plants is not considered solely as an antifungal resistance mechanism. We discuss the importance of chitin forms and chitinases in the plant-fungal interactions and their role in persistent and possible biocontrol.
chitosan, chitin, chitinase, PR protein, plant–fungal interaction
Structure type: structural motif or average structure
Location inside paper: fig. 1
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
Biological activity: induces host defence responses in plants; induces expression of PR(pathogenesis-related) proteins; functions as MAMP(microbe-associated molecular pattern; binds with LysM RLKs
Related record ID(s): 49146
NCBI Taxonomy refs (TaxIDs): 5544,
29911,
5518,
62690,
40559,
5180,
38451,
39291Reference(s) to other database(s): GTC:G97099AY
Show glycosyltransferases
There is only one chemically distinct structure: