@article{mbs:/content/journal/micro/10.1099/mic.0.26301-0, author = "Garcerá, Ana and Martínez, Ana Isabel and Castillo, Luis and Elorza, M. Victoria and Sentandreu, Rafael and Valentín, Eulogio", title = "Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein", journal= "Microbiology", year = "2003", volume = "149", number = "8", pages = "2137-2145", doi = "https://doi.org/10.1099/mic.0.26301-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.26301-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "CR, Congo red", keywords = "IPF, individual protein file", keywords = "GPI, glycosylphosphatidylinositol", keywords = "CW, calcofluor white", 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-β-glucanase) and therefore seems to be covalently linked to the β-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 β-glucan.", }