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

作者:Mille Celine; Fradin Chantal; Delplace Florence; Trinel Pierre Andre; Masset Annick; Francois Nadine; Coddeville Bernadette; Bobrowicz Piotr; Jouault Thierry; Guerardel Yann; Wildt Stefan; Janbon Guilhem; Poulain Daniel*
来源:Glycobiology, 2012, 22(10): 1332-1342.
DOI:10.1093/glycob/cws097

摘要

A family of nine genes encoding proteins involved in the synthesis of beta-1,2 mannose adhesins of Candida albicans has been identified. Four of these genes, BMT1-4, encode enzymes acting stepwise to add beta-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 beta-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 beta-oligomannoside chain, respectively. Disruptions had no effect on sphingolipid biosynthesis and on PPM beta-mannosylation. beta-Mannose surface expression was not affected, confirming that beta-mannosylation is a process based on specificity of acceptor molecules, but liable to global regulation.

  • 出版日期2012-10