Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 16710478Publication DOI: 10.1172/JCI27114Journal NLM ID: 7802877Publisher: Ann Arbor, MI: American Society for Clinical Investigation
Correspondence: Netea MG <m.netea
aig.umcn.nl>
Institutions: School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK, Department of Medicine, Radboud University, Nijmegen Medical Centre, Nijmegen, The Netherlands, Nijmegen University, Center for Infectious Diseases, Nijmegen, The Netherlands, Department of Tumor Immunology, Radboud University, Nijmegen Medical Centre, Nijmegen, The Netherlands, Department of Surgery, East Tennessee State University, Johnson City, USA
The fungal pathogen Candida albicans has a multilayered cell wall composed of an outer layer of proteins glycosylated with N- or O-linked mannosyl residues and an inner skeletal layer of β-glucans and chitin. We demonstrate that cytokine production by human mononuclear cells or murine macrophages was markedly reduced when stimulated by C. albicans mutants defective in mannosylation. Recognition of mannosyl residues was mediated by mannose receptor binding to N-linked mannosyl residues and by TLR4 binding to O-linked mannosyl residues. Residual cytokine production was mediated by recognition of β-glucan by the dectin-1/TLR2 receptor complex. C. albicans mutants with a cell wall defective in mannosyl residues were less virulent in experimental disseminated candidiasis and elicited reduced cytokine production in vivo. We concluded that recognition of C. albicans by monocytes/macrophages is mediated by 3 recognition systems of differing importance, each of which senses specific layers of the C. albicans cell wall.
lectin, Candida albicans, beta-glucan, Dectin-1, lectin receptor, cytokine production, TLR2
Structure type: oligomer
Location inside paper: Fig. 1, G
Aglycon: (->3) Ser/Thr-protein
Compound class: O-polysaccharide, cell wall polysaccharide, mannan
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164480,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
Methods: biological assays, extraction, antibody binding, cytokine production, TEM, macrophage production
Enzymes that release or process the structure: mnt1, mnt2, pmr1
Related record ID(s): 44265
NCBI Taxonomy refs (TaxIDs): 5476Reference(s) to other database(s): GTC:G95196FC
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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