Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
The structure was elucidated in this paperNCBI PubMed ID: 27568483Publication DOI: 10.1111/cmi.12659Journal NLM ID: 100883691Publisher: Oxford: Wiley-Blackwell
Correspondence: s.j.gurr
exeter.ac.uk
Institutions: Department of Plant Sciences, University of Oxford, Oxford, UK, Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), Stockholm, Sweden, Centre for Plant Biotechnology and Genomics, Universidad Politécnica de Madrid, Madrid, Spain, ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, University of Adelaide, Urrbrae, Australia, School of Biosciences, College of Life and Environmental Sciences, University of Exeter, Exeter, UK
The fungal wall is pivotal for cell shape and function, and in interfacial protection during host infection and environmental challenge. Here, we provide the first description of the carbohydrate composition and structure of the cell wall of the rice blast fungus Magnaporthe oryzae. We focus on the family of glucan elongation proteins (Gels) and characterize five putative β-1,3-glucan glucanosyltransferases that each carry the Glycoside Hydrolase 72 signature. We generated targeted deletion mutants of all Gel isoforms, that is, the GH72+ , which carry a putative carbohydrate-binding module, and the GH72- Gels, without this motif. We reveal that M. oryzae GH72+ GELs are expressed in spores and during both infective and vegetative growth, but each individual Gel enzymes are dispensable for pathogenicity. Further, we demonstrated that a Δgel1Δgel3Δgel4 null mutant has a modified cell wall in which 1,3-glucans have a higher degree of polymerization and are less branched than the wild-type strain. The mutant showed significant differences in global patterns of gene expression, a hyper-branching phenotype and no sporulation, and thus was unable to cause rice blast lesions (except via wounded tissues). We conclude that Gel proteins play significant roles in structural modification of the fungal cell wall during appressorium-mediated plant infection.
Structure type: homopolymer
Location inside paper: Figure 6(1,3-Glcp), 1,3-glucan
Trivial name: glucan, β-1,3-glucan, curdlan, curdlan-type polysaccharide 13140, paramylon, curdlan, laminarin, β-glucan, curdlan, β-(1,3)-glucan, β-(1,3)-glucan, curdlan, curdlan, β-1,3-glucan, paramylon, reserve polysaccharide, b-glucan, β-1,3-D-glucan, laminaran, botryosphaeran, laminaran type β-D-glucan, latiglucan I, pachymaran, Curdlan, zymosan A, β-glucan, curdlan, laminarin, zymosan, zymosan, glucan particles, zymosan, β-(1-3)-glucan, β-(1,3)-glucan, β-(1,3)glucan, pachymaran, D-glucan (DPn)540, pachyman, laminaran, curdlan, zymosan, zymosan, β-(1,3)-glucan, zymosan A, zymosan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, β-1,3-glucan, curdlan, pachyman, β-(1,3)-glucan, curdlan, callose, a water-insoluble β-(1→3)-glucan, fermentum β-polysaccharide, water-insoluble glucan, alkali-soluble β-glucan (PeA3), alkali-soluble polysaccharide (PCAP), callose, laminarin
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, lipophosphoglycan, glycoprotein, LPG, glucan, polysaccharide, glycoside, β-glucan, β3-glucan, cell wall glucan
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_2278476,IEDB_2278477,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Methods: methylation, GC-EI-MS, acid hydrolysis, biological assays, acetylation, cell growth, RNA sequencing, confocal microscopy, SEM, TEM
Enzymes that release or process the structure: Gel family of β-1,3-glucanosyltransferases
Comments, role: cell wall component
Related record ID(s): 43186, 43187
NCBI Taxonomy refs (TaxIDs): 318829Reference(s) to other database(s): GTC:G51056AN, GlycomeDB:
157, CCSD:
50049, CBank-STR:4225, CA-RN: 51052-65-4, GenDB:FJ3380871.1
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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