Taxonomic group: fungi / Ascomycota, Ascomycota, Ascomycota, Basidiomycota, Ascomycota, Ascomycota
(Phylum: Ascomycota, Ascomycota, Ascomycota, Basidiomycota, Ascomycota, Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 24244155Publication DOI: 10.1371/journal.ppat.1003716Journal NLM ID: 101238921Publisher: San Francisco, CA: Public Library of Science
Correspondence: anne.beauvais
pasteur.fr
Institutions: School of Life Sciences, Arizona State University, Tempe, USA, Unité des Aspergillus, Institut Pasteur, Paris, France, Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Perugia, Italy, Molecular and Applied Microbiology, Leibniz-Institute for Natural Product Research and Infection Biology (HKI), University of Jena, Jena, Germany, Integrated Research and Treatment Center, Center for Sepsis Control and Care Jena, University Hospital (CSCC), Jena, Germany, CNRS, LAAS, Toulouse, France, 6 Unité de Défence Inneé et Inflammation, Institut Pasteur, Paris, France
α-(1,3)-Glucan is a major component of the cell wall of Aspergillus fumigatus, an opportunistic human fungal pathogen. There are three genes (AGS1, AGS2 and AGS3) controlling the biosynthesis of α-(1,3)-glucan in this fungal species. Deletion of all the three AGS genes resulted in a triple mutant that was devoid of α-(1,3)-glucan in its cell wall; however, its growth and germination was identical to that of the parental strain in vitro. In the experimental murine aspergillosis model, this mutant was less pathogenic than the parental strain. The AGS deletion resulted in an extensive structural modification of the conidial cell wall, especially conidial surface where the rodlet layer was covered by an amorphous glycoprotein matrix. This surface modification was responsible for viability reduction of conidia in vivo, which explains decrease in the virulence of triple agsΔ mutant.
Structure type: homopolymer
Location inside paper: p. 1, column 1, paragraph 1
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, callose, laminarin, alkali-soluble β-glucan (PeA3), alkali-soluble polysaccharide (PCAP)
Compound class: EPS, O-polysaccharide, cell wall polysaccharide, lipophosphoglycan, glycoprotein, LPG, glucan, cell wall glucan, polysaccharide, glycoside, β-glucan, β-1, 3-glucan
Contained glycoepitopes: IEDB_1397514,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_161166,IEDB_558869,IEDB_857743,IEDB_983931,SB_192
Methods: fluorescence microscopy, TEM, AFM
Enzymes that release or process the structure: Ags1p, Ags2p, Ags3p
Biosynthesis and genetic data: biochemical data, genetic data
Related record ID(s): 44857, 44887, 44908, 44926, 44938
NCBI Taxonomy refs (TaxIDs): 121759,
5037,
5039,
5207,
746128Reference(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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