Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 149 (2003), 2137-2145; DOI  10.1099/mic.0.26301-0
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary data
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Garcerá, A.
Right arrow Articles by Valentín, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Garcerá, A.
Right arrow Articles by Valentín, E.
Agricola
Right arrow Articles by Garcerá, A.
Right arrow Articles by Valentín, E.
Microbiology 149 (2003), 2137-2145; DOI  10.1099/mic.0.26301-0
© 2003 Society for General Microbiology

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

Ana Garcerá, Ana Isabel Martínez, Luis Castillo, M. Victoria Elorza, Rafael Sentandreu and Eulogio Valentín

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-{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.


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.




This article has been cited by other articles:


Home page
Microbiol. Mol. Biol. Rev.Home page
W. L. Chaffin
Candida albicans Cell Wall Proteins
Microbiol. Mol. Biol. Rev., September 1, 2008; 72(3): 495 - 544.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
G. J. Sosinska, P. W. J. de Groot, M. J. Teixeira de Mattos, H. L. Dekker, C. G. de Koster, K. J. Hellingwerf, and F. M. Klis
Hypoxic conditions and iron restriction affect the cell-wall proteome of Candida albicans grown under vagina-simulative conditions
Microbiology, February 1, 2008; 154(2): 510 - 520.
[Abstract] [Full Text] [PDF]


Home page
Eukaryot CellHome page
M. L. Richard and A. Plaine
Comprehensive Analysis of Glycosylphosphatidylinositol-Anchored Proteins in Candida albicans
Eukaryot. Cell, February 1, 2007; 6(2): 119 - 133.
[Full Text] [PDF]


Home page
Eukaryot CellHome page
P. W. J. de Groot, A. D. de Boer, J. Cunningham, H. L. Dekker, L. de Jong, K. J. Hellingwerf, C. de Koster, and F. M. Klis
Proteomic Analysis of Candida albicans Cell Walls Reveals Covalently Bound Carbohydrate-Active Enzymes and Adhesins
Eukaryot. Cell, August 1, 2004; 3(4): 955 - 965.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 2003 Society for General Microbiology.