Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 25467440Publication DOI: 10.1128/mBio.01874-14Journal NLM ID: 101519231Publisher: Washington, DC: American Society for Microbiology
Correspondence: Bain JM <jude.bain
abdn.ac.uk>
Institutions: Aberdeen Fungal Group, University of Aberdeen, Aberdeen, UK
Candida albicans is a major life-threatening human fungal pathogen in the immunocompromised host. Host defense against systemic Candida infection relies heavily on the capacity of professional phagocytes of the innate immune system to ingest and destroy fungal cells. A number of pathogens, including C. albicans, have evolved mechanisms that attenuate the efficiency of phagosome-mediated inactivation, promoting their survival and replication within the host. Here we visualize host-pathogen interactions using live-cell imaging and show that viable, but not heat- or UV-killed C. albicans cells profoundly delay phagosome maturation in macrophage cell lines and primary macrophages. The ability of C. albicans to delay phagosome maturation is dependent on cell wall composition and fungal morphology. Loss of cell wall O-mannan is associated with enhanced acquisition of phagosome maturation markers, distinct changes in Rab GTPase acquisition by the maturing phagosome, impaired hyphal growth within macrophage phagosomes, profound changes in macrophage actin dynamics, and ultimately a reduced ability of fungal cells to escape from macrophage phagosomes. The loss of cell wall O-mannan leads to exposure of β-glucan in the inner cell wall, facilitating recognition by Dectin-1, which is associated with enhanced phagosome maturation.
cell wall, β-glucan, Candida albicans, b-glucan
Structure type: homopolymer
Location inside paper: pg. 2, column 1, line 45
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
Comments, role: This β-1,3-glucan linked to chitin. The article does not possess any information on β-1,3-glucan structure.
Related record ID(s): 46323, 46325
NCBI Taxonomy refs (TaxIDs): 5476Reference(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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