Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Associated disease: infection due to Histoplasma capsulatum [ICD11:
XN8VH 
]
NCBI PubMed ID: 28513415Publication DOI: 10.1128/microbiolspec.FUNK-0035-2016Journal NLM ID: 101634614Publisher: Washington, DC: ASM Press
Correspondence: n.gow
abdn.ac.uk
Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France, Aberdeen Fungal Group, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK
The molecular composition of the cell wall is critical for the biology and ecology of each fungal species. Fungal walls are composed of matrix components that are embedded and linked to scaffolds of fibrous load-bearing polysaccharides. Most of the major cell wall components of fungal pathogens are not represented in humans, other mammals, or plants, and therefore the immune systems of animals and plants have evolved to recognize many of the conserved elements of fungal walls. For similar reasons the enzymes that assemble fungal cell wall components are excellent targets for antifungal chemotherapies and fungicides. However, for fungal pathogens, the cell wall is often disguised since key signature molecules for immune recognition are sometimes masked by immunologically inert molecules. Cell wall damage leads to the activation of sophisticated fail-safe mechanisms that shore up and repair walls to avoid catastrophic breaching of the integrity of the surface. The frontiers of research on fungal cell walls are moving from a descriptive phase defining the underlying genes and component parts of fungal walls to more dynamic analyses of how the various components are assembled, cross-linked, and modified in response to environmental signals. This review therefore discusses recent advances in research investigating the composition, synthesis, and regulation of cell walls and how the cell wall is targeted by immune recognition systems and the design of antifungal diagnostics and therapeutics.
Structure type: homopolymer
Location inside paper: β-(1,3)glucan, Figure 1f, ref.[12],[24],[26]
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
Biological activity: outer wall layer of α-(1,3)glucan prevents efficient dectin-1-mediated immune recognition of β-(1,3) glucan in the inner cell wall; in C. albicans and S. cerevisiae β-(1,6) glucan acts as a linker molecule binding cell wall proteins (CWPs) to the β-(1,3) glucan-chitin skeleton via a glycosylphosphatidyl inositol (GPI) remnant; component of biofilms formed by extracellular matrix of C. albicans growed on solid surfaces
Related record ID(s): 40724, 43188, 43190, 43191, 43192, 43193, 43194, 43198, 43199, 43200, 43201, 43203, 43204, 43205
NCBI Taxonomy refs (TaxIDs): 5037,
5476,
4932Reference(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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(previously named: Ajellomyces capsulata, Cryptococcus capsulatus, Emmonsiella capsulata, Ajellomyces capsulatas)