Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
The structure was elucidated in this paperNCBI PubMed ID: 15519997Publication DOI: 10.1074/jbc.M411413200Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: n.gow
abdn.ac.uk
Institutions: School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen, UK, School of Life Sciences, Wellcome Trust Building, University of Dundee, Dundee, UK, AstraZeneca R and D Boston, Waltham, MA, USA, Molecular and Cellular Biology Building, University of Minnesota, Minneapolis, USA, Division of Medical Mycology, Department of Microbiology and Immunology, Medical University of South Carolina, Charleston, USA, Department of Medical Microbiology, Polwarth Building, University of Aberdeen, Aberdeen, UK
The MNT1 gene of the human fungal pathogen Candida albicans is involved in O-glycosylation of cell wall and secreted proteins and is important for adherence of C. albicans to host surfaces and for virulence. Here we describe the molecular analysis of CaMNT2, a second member of the MNT1-like gene family in C. albicans. Mnt2p also functions in O-glycosylation. Mnt1p and Mnt2p encode partially redundant α-1,2-mannosyltransferases that catalyze the addition of the second and third mannose residues in an O-linked man no se pentamer. Deletion of both copies of MNT1 and MNT2 resulted in reduction in the level of in vitro mannosyltransferase activity and truncation of O-mannan. Both the mnt2Δ and mnt1Δ single mutants were significantly reduced in adherence to human buccal epithelial cells and Matrigel-coated surfaces, indicating a role for O-glycosylated cell wall proteins or O-mannan itself in adhesion to host surfaces. The double mnt1Δmnt2Δ mutant formed aggregates of cells that appeared to be the result of abnormal cell separation. The double mutant was attenuated in virulence, underlining the importance of O-glycosylation in pathogenesis of C. albicans infections.
Candida albicans, α-1, fungal pathogen, gene deletion, 2-mannosyltransferase
Structure type: oligomer
Location inside paper: Fig.9
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: methylation, DNA sequencing, GC-MS, TLC, HPAEC, biological assays, radiolabeling, enzymatic digestion, HPAEC-PAD, extraction, cloning, ESI-QTOF-MS, cell growth, enzymatic assay, reductive beta-elimination, TEM, beta-elimination
Enzymes that release or process the structure: Mnt1p, Mnt2p, Pmt1p, Pmt2p, Pmt3p, Pmt4p, Pmt5p, α-1,2-mannosidase
Related record ID(s): 44360, 44361, 44362
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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