Literature DB >> 12904553

Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein.

Ana Garcerá1, Ana Isabel Martínez1, Luis Castillo1, M Victoria Elorza1, Rafael Sentandreu1, Eulogio Valentín1.   

Abstract

After screening of a Candida albicans genome database, the product of an ORF (IPF 3054) that has 62 % homology with Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-beta-glucanase) and therefore seems to be covalently linked to the beta-glucan of the cell walls. Both disruption and overexpression of the CaSSR1 gene caused an increased sensitivity to calcofluor white, Congo red and zymolyase digestion. These results suggest that CaSsr1p has a structural role associated with the cell-wall beta-glucan.

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Year:  2003        PMID: 12904553     DOI: 10.1099/mic.0.26301-0

Source DB:  PubMed          Journal:  Microbiology        ISSN: 1350-0872            Impact factor:   2.777


  8 in total

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4.  Proteomic analysis of Candida albicans cell walls reveals covalently bound carbohydrate-active enzymes and adhesins.

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Authors:  Zhuo Zhou; Zoe Jordens; Shuguang Zhang; Ningxin Zhang; Jan Schmid
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Review 6.  Evolutionary Overview of Molecular Interactions and Enzymatic Activities in the Yeast Cell Walls.

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7.  Functional analysis of Candida albicans GPI-anchored proteins: roles in cell wall integrity and caspofungin sensitivity.

Authors:  Armêl Plaine; Louise Walker; Gregory Da Costa; Héctor M Mora-Montes; Alastair McKinnon; Neil A R Gow; Claude Gaillardin; Carol A Munro; Mathias L Richard
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  8 in total

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