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

Departamento de Microbiología y Ecología, Facultad de Farmacia, Universidad de Valencia, Avda. Vicente Andrés Estellés s/n, 46100-Burjassot (Valencia), Spain Correspondence Eulogio Valentin Eulogio.Valentin{at}uv.es After screening of a Candida albicans genome database, the product of an ORF (IPF 30...

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Published in:Microbiology (Society for General Microbiology) 2003-08, Vol.149 (8), p.2137-2145
Main Authors: Garcera, Ana, Martinez, Ana Isabel, Castillo, Luis, Elorza, M. Victoria, Sentandreu, Rafael, Valentin, Eulogio
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description Departamento de Microbiología y Ecología, Facultad de Farmacia, Universidad de Valencia, Avda. Vicente Andrés Estellés s/n, 46100-Burjassot (Valencia), Spain Correspondence Eulogio Valentin Eulogio.Valentin{at}uv.es 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- -glucanase) and therefore seems to be covalently linked to the -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 -glucan. Abbreviations: CR, Congo red; CW, calcofluor white; GPI, glycosylphosphatidylinositol; IPF, individual protein file A table showing putative GPI-proteins in Candida albicans can be found in Microbiology Online.
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Vicente Andrés Estellés s/n, 46100-Burjassot (Valencia), Spain Correspondence Eulogio Valentin Eulogio.Valentin{at}uv.es 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- -glucanase) and therefore seems to be covalently linked to the -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 -glucan. 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subjects Amino Acid Sequence
Base Sequence
beta -Glucan
Biological and medical sciences
Candida albicans
Candida albicans - genetics
Cell Wall - metabolism
Cloning, Molecular
DNA, Fungal - genetics
Fundamental and applied biological sciences. Psychology
Fungal Proteins - genetics
Gene Deletion
Gene Expression
Growth, nutrition, metabolism, transports, enzymes. Molecular biology
Microbiology
Molecular Sequence Data
Mycology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae Proteins - genetics
Sequence Homology, Amino Acid
Species Specificity
Ssr1 protein
zymolyase
title Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein
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