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© Institut Pasteur
Cryptococcus neoformans
Publication : Glycobiology

Members 5 and 6 of the Candida albicans BMT family encode enzymes acting specifically on β-mannosylation of the phospholipomannan cell-wall glycosphingolipid

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Glycobiology - 27 Jun 2012

Mille C, Fradin C, Delplace F, Trinel PA, Masset A, François N, Coddeville B, Bobrowicz P, Jouault T, Guerardel Y, Wildt S, Janbon G, Poulain D

Link to Pubmed [PMID] – 22745283

Glycobiology 2012 Oct;22(10):1332-42

A family of nine genes encoding proteins involved in the synthesis of β-1,2 mannose adhesins of Candida albicans has been identified. Four of these genes, BMT1-4, encode enzymes acting stepwise to add β-mannoses on to cell-wall phosphopeptidomannan (PPM). None of these acts on phospholipomannan (PLM), a glycosphingolipid member of the mannose-inositol-phosphoceramide family, which contributes with PPM to β-mannose surface expression. We show that deletion of BMT5 and BMT6 led to a dramatic reduction of PLM glycosylation and accumulation of PLM with a truncated β-oligomannoside chain, respectively. Disruptions had no effect on sphingolipid biosynthesis and on PPM β-mannosylation. β-Mannose surface expression was not affected, confirming that β-mannosylation is a process based on specificity of acceptor molecules, but liable to global regulation.