Document Detail

Localisation of Bgl2p upon antifungal drug treatment in Candida albicans.
MedLine Citation:
PMID:  19013773     Owner:  NLM     Status:  MEDLINE    
Several proteins are covalently bound to the cell wall glucan (glucan-associated proteins (GAPs)) in Candida albicans and different drugs may cause their modulation. Proteomic analysis is a suitable approach to study differential GAP patterns between control and drug-treated cells. Since antimycotics induce variation in GAP content, we investigated the effect of a sublethal dose of micafungin and observed a clear increase in Bgl2p, an enzyme with glucanosyltransferase activity, with respect to a general decrease in cell wall protein content. Immunoelectron microscopy using mouse antiserum confirmed this increase of Bgl2p on the outer cell wall but also revealed a dramatic increase in the immature Bgl2p isoform in the cytoplasm of drug-treated cells. Since this increased expression of Bgl2p is clearly dependent upon micafungin treatment, this enzyme appears to be one of the survival strategies of C. albicans and thus could be considered the molecular basis of antifungal resistance and also as a potential valuable candidate for future vaccine development.
Letizia Angiolella; Alberto Vitali; Annarita Stringaro; Giuseppina Mignogna; Bruno Maras; Mariantonietta Bonito; Marisa Colone; Anna Teresa Palamara; Antonio Cassone
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Publication Detail:
Type:  Journal Article     Date:  2008-11-14
Journal Detail:
Title:  International journal of antimicrobial agents     Volume:  33     ISSN:  0924-8579     ISO Abbreviation:  Int. J. Antimicrob. Agents     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2009-01-12     Completed Date:  2009-03-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9111860     Medline TA:  Int J Antimicrob Agents     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  143-8     Citation Subset:  IM    
Department of Public Health Sciences G. Sanarelli, University of Rome La Sapienza, Rome, Italy.
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MeSH Terms
Antifungal Agents / pharmacology*
Candida albicans / chemistry,  drug effects*
Cell Wall / chemistry
Cytoplasm / chemistry
Echinocandins / pharmacology*
Fungal Proteins / biosynthesis*
Glucosyltransferases / biosynthesis*
Lipopeptides / pharmacology*
Microscopy, Immunoelectron
Proteome / analysis,  drug effects
Reg. No./Substance:
0/Antifungal Agents; 0/Echinocandins; 0/Fungal Proteins; 0/Lipopeptides; 0/Proteome; 0/micafungin; EC 2.4.1.-/Glucosyltransferases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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