This Article Full Text (PDF) Other Versions of this Article: IAI.00368-08v1 76/10/4509    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Fradin, C. Articles by Poulain, D. PubMed PubMed Citation Articles by Fradin, C. Articles by Poulain, D.

 Previous Article  |  Next Article 

Infect. Immun. doi:10.1128/IAI.00368-08
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

-1,2 oligomannose adhesin epitopes are widely distributed over the different families of Candida albicans cell wall mannoproteins and are associated through both N- and O-glycosylation processes

U M R Inserm 799, Laboratoire de Mycologie Fondamentale et Appliquée; Université de Lille2, 59045, Lille cedex, France; Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, 59655, Villeneuve d'Ascq, France; Groupe d'Etude des Interactions Hôte-Pathogène, UPRES EA 3142, UFR des Sciences Pharmaceutiques et d'Ingénierie de la Santé, 16 bd Daviers, 49000 Angers, France; Institut für Mikrobiologie, Heinrich-Heine-Universität, Universitätsstr. 1/26.12. D-40225 Düsseldorf, Germany

^* To whom correspondence should be addressed. Email: dpoulain{at}univ-lille2.fr.

	Abstract

-1,2 linked mannosides (-Mans) are believed to contribute to Candida albicans virulence. The presence of -Mans has been chemically established in two molecules non-covalently linked to the cell wall, phosphopeptidomannan (PPM) and phospholipomannan (PLM), where they correspond to specific epitopes. However, a large number of cell wall mannoproteins (CWMPs) also express -Man epitopes, although their nature and mode of -mannosylation is unknown. We therefore use western blotting to map -Man epitopes on the different families of MPs gradually released from the cell wall according to their mode of anchorage (soluble, released by dithiothreitol (DTT), -1,3 glucan linked and -1,6 glucan linked). Reduction of -Man epitope expression occurred after chemical and enzymatic deglycosylation of the different cell wall fractions, as well as in a secreted form of Hwp1, a representative member of CWMPs linked by GPI remnants. ELISA inhibition tests were performed to assess the presence of -Man epitopes in released oligomannosides. A comparison of the results obtained with CWMPs to those obtained with PPM and the use of mutants affected in O- and N-glycosylation demonstrated that both O- and N-glycosylation participate in the association of -Mans with the protein moieties of CWMPs. This process, which can alter the function of cell wall molecules and their recognition by the host, is therefore more important and more complex than originally thought, since it differs from the model established previously with PPM.