Document Detail


Molecular phenotyping of mannosyltransferases-deficient Candida albicans cells by high-resolution magic angle spinning NMR.
MedLine Citation:
PMID:  19218187     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The yeast Candida albicans is an opportunistic pathogen that causes infections in immunocompromised individuals with a high morbidity and mortality levels. Recognition of yeasts by host cells is directly mediated by cell wall components of the yeast, including a wide range of abundantly expressed glycoconjugates. Of particular interest in C. albicans are the beta-mannosylated epitopes that show a complex expression pattern on N-glycan moiety of phosphopeptidomannans and are absent in the non-pathogenic species Saccharomyces cerevisiae. Being known as potent antigens for the adaptive immune response and elicitors of specific infection-protective antibodies, the exact delineation of beta-mannosides regulation and expression pathways has lately become a major milestone toward the comprehension of host-pathogen interplay. Using the newly developed HR-MAS NMR methodology, we demonstrate the possibility of assessing the general profiles of cell-surface-exposed glycoconjugates from intact living yeast cells without any prior purification step. This technique permitted to directly observe structural modifications of surface expressed phosphodiester-linked beta-mannosides on a series of deletion strains in beta-mannosyltransferases and phospho-mannosyltransferases compared with their parental strains.
Authors:
Emmanuel Maes; Céline Mille; Xavier Trivelli; Guilhem Janbon; Daniel Poulain; Yann Guérardel
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-01-17
Journal Detail:
Title:  Journal of biochemistry     Volume:  145     ISSN:  1756-2651     ISO Abbreviation:  J. Biochem.     Publication Date:  2009 Apr 
Date Detail:
Created Date:  2009-04-06     Completed Date:  2009-07-06     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  England    
Other Details:
Languages:  eng     Pagination:  413-9     Citation Subset:  IM    
Affiliation:
Unité de Glycobiologie Structurale et Fonctionnelle, UMR CNRS 8576, IFR 147, Université des Sciences et Technologies de Lille 1, 59655, Villeneuve d'Ascq, France.
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MeSH Terms
Descriptor/Qualifier:
Candida albicans / cytology*,  enzymology*
Magnetic Resonance Spectroscopy
Mannans / chemistry,  isolation & purification
Mannosyltransferases / deficiency*
Models, Molecular*
Phenotype
Phosphopeptides / chemistry,  isolation & purification
Polysaccharides / chemistry
Solubility
Chemical
Reg. No./Substance:
0/Mannans; 0/Phosphopeptides; 0/Polysaccharides; 0/phosphopeptidomannan; EC 2.4.1.-/Mannosyltransferases

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