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J Biol Chem, Vol. 274, Issue 43, 30520-30526, October 22, 1999

The Candida albicans Phospholipomannan Is a Family of Glycolipids Presenting Phosphoinositolmannosides with Long Linear Chains of beta -1,2-Linked Mannose Residues

Pierre-André TrinelDagger , Yves Plancke§, Peter Gerold, Thierry JouaultDagger , Florence Delplace§, Ralph T. Schwarz, Gérard Strecker§, and Daniel PoulainDagger

From the Dagger  Equipe Mixte de l'INSERM 99-15, Laboratoire de Mycologie Fondamentale et Appliquée, Faculté de Médecine, Centre Hospitalier Universitaire, Place de Verdun, 59045 Lille Cedex, France, § Laboratoire de Chimie Biologique et Unité Mixte 111, CNRS, Université de Lille I, 59655 Villeneuve d'Ascq Cedex, France, and  Zentrum für Hygiene und Medizinische Mikrobiologie, Philipps-Universität Marburg, Robert Koch Strasse 17, 35037 Marburg, Germany

In a series of studies, we have shown that Candida albicans synthesizes a glycolipid, phospholipomannan (PLM), which reacted with antibodies specific for beta -1,2-oligomannosides and was biosynthetically labeled by [3H]mannose, [3H]palmitic acid, and [32P]phosphorus. PLM has also been shown to be released from the C. albicans cell wall and to bind to and stimulate macrophage cells. In this study, we show by thin layer chromatography scanning of metabolically radiolabeled extracts that the C. albicans PLM corresponds to a family of mannose and inositol co-labeled glycolipids. We describe the purification process of the molecule and the release of its glycan fraction through alkaline hydrolysis. Analysis of this glycan fraction by radiolabeling and methylation-methanolysis confirmed the presence of inositol and of 1,2-linked mannose units. NMR studies evidenced linear chains of beta -1,2-oligomannose as the major PLM components. Mass spectrometry analysis revealed that these chains were present in phosphoinositolmannosides with degrees of polymerization varying from 8 to 18 sugar residues. The PLM appears as a new type of eukaryotic inositol-tagged glycolipid in relationship to both the absence of glucosamine and the organization of its glycan chains. This first structural evidence for the presence of beta -1,2-oligomannosides in a glycoconjugate other than the C. albicans phosphopeptidomannan may have some pathophysiological relevance to the adhesive, protective epitope, and signaling properties thus far established for these residues.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.



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