Document Detail


Beta-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.
MedLine Citation:
PMID:  18644880     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Beta-1,2-linked mannosides (beta-Mans) are believed to contribute to Candida albicans virulence. The presence of beta-Mans has been chemically established for two molecules (phosphopeptidomannan [PPM] and phospholipomannan) that are noncovalently linked to the cell wall, where they correspond to specific epitopes. However, a large number of cell wall mannoproteins (CWMPs) also express beta-Man epitopes, although their nature and mode of beta-mannosylation are unknown. We therefore used Western blotting to map beta-Man epitopes for the different families of mannoproteins gradually released from the cell wall according to their mode of anchorage (soluble, released by dithiothreitol, beta-1,3 glucan linked, and beta-1,6 glucan linked). Reduction of beta-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 of the CWMPs linked by glycosylphosphatidylinositol remnants. Enzyme-linked immunosorbent assay inhibition tests were performed to assess the presence of beta-Man epitopes in released oligomannosides. A comparison of the results obtained with CWMPs to the results obtained with PPM and the use of mutants with mutations affecting O and N glycosylation demonstrated that both O glycosylation and N glycosylation participate in the association of beta-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.
Authors:
Chantal Fradin; Marie Christine Slomianny; Céline Mille; Annick Masset; Raymond Robert; Boualem Sendid; Joachim F Ernst; Jean Claude Michalski; Daniel Poulain
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-07-21
Journal Detail:
Title:  Infection and immunity     Volume:  76     ISSN:  1098-5522     ISO Abbreviation:  Infect. Immun.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-09-18     Completed Date:  2008-10-16     Revised Date:  2013-06-05    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4509-17     Citation Subset:  IM    
Affiliation:
UMR Inserm 799, Laboratoire de Mycologie Fondamentale et Appliquée, Universitéde Lille 2, 59045 Lille cedex, France.
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MeSH Terms
Descriptor/Qualifier:
Antibodies, Fungal / metabolism
Antibodies, Monoclonal / metabolism
Blotting, Western
Candida albicans / chemistry,  immunology*
Cell Wall / chemistry,  immunology*
Enzyme-Linked Immunosorbent Assay
Epitope Mapping
Epitopes / immunology*
Fungal Proteins / chemistry,  immunology*
Glycosylation
Mannosides / immunology
Membrane Glycoproteins / chemistry,  immunology*
Protein Binding
Virulence Factors / chemistry,  immunology*
Chemical
Reg. No./Substance:
0/Antibodies, Fungal; 0/Antibodies, Monoclonal; 0/Epitopes; 0/Fungal Proteins; 0/Mannosides; 0/Membrane Glycoproteins; 0/Virulence Factors; 0/mannoproteins
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