Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 29452950Publication DOI: 10.1016/j.tim.2018.01.007Journal NLM ID: 9310916Publisher: Cambridge: Elsevier Trends Journals
Correspondence: robert.wheeler1
maine.edu
Institutions: Molecular & Biomedical Sciences, University of Maine, Orono, USA, MRC Centre for Medical Mycology, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK, Institute of Microbiologyand Infection, and School of Biosciences, University of Birmingham, Edgbaston, Birmingham, UK, Graduate School of Biomedical Sciences and Engineering, University of Maine, Orono, USA
Deadly infections from opportunistic fungi have risen in frequency, largely because of the at-risk immunocompromised population created by advances in modern medicine and the HIV/AIDS pandemic. This review focuses on dynamics of the fungal polysaccharide cell wall, which plays an outsized role in fungal pathogenesis and therapy because it acts as both an environmental barrier and as the major interface with the host immune system. Human fungal pathogens use architectural strategies to mask epitopes from the host and prevent immune surveillance, and recent work elucidates how biotic and abiotic stresses present during infection can either block or enhance masking. The signaling components implicated in regulating fungal immune recognition can teach us how cell wall dynamics are controlled, and represent potential targets for interventions designed to boost or dampen immunity.
cell wall, glucan, innate immunity, fungi, evasion
Structure type: structural motif or average structure
Location inside paper: p. 288, paragraph 6
Trivial name: β-1,3-glucan
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, 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
Biological activity: functions as PAMP (pathogen-associated molecular pattern); composes the inner layer of cell wall; binds to Dectin-1 and Dectin-2
Enzymes that release or process the structure: FKS1
Related record ID(s): 48715, 48716
NCBI Taxonomy refs (TaxIDs): 121759,
746128Reference(s) to other database(s): GTC:G51056AN
Show glycosyltransferases
There is only one chemically distinct structure:
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