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Eukaryotic Cell, January 2006, p. 140-147, Vol. 5, No. 1
1535-9778/06/$08.00+0     doi:10.1128/EC.5.1.140-147.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Candida albicans Ecm33p Is Important for Normal Cell Wall Architecture and Interactions with Host Cells

Raquel Martinez-Lopez,1 Hyunsook Park,2 Carter L. Myers,2 Concha Gil,1 and Scott G. Filler2,3*

Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense de Madrid, Plaza de Ramón y Cajal s/n, 28040-Madrid, Spain,1 St. Johns Cardiovascular Research Center, Division of Infectious Diseases, Department of Medicine, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, Torrance, California 90502,2 The David Geffen School of Medicine at UCLA, Los Angeles, California 900243

Received 2 September 2005/ Accepted 8 November 2005

Candida albicans ECM33 encodes a glycosylphosphatidylinositol-linked cell wall protein that is important for cell wall integrity. It is also critical for normal virulence in the mouse model of hematogenously disseminated candidiasis. To identify potential mechanisms through which Ecm33p contributes to virulence, we investigated the interactions of C. albicans ecm33{Delta} mutants with endothelial cells and the FaDu oral epithelial cell line in vitro. The growth rate of blastospores of strains containing either one or no intact copies of ECM33 was 50% slower than that of strains containing two intact copies of ECM33. However, all strains germinated at the same rate, forming similar-length hyphae on endothelial cells and oral epithelial cells. Strains containing either one or no intact copies of ECM33 had modestly reduced adherence to both types of host cells, and a markedly reduced capacity to invade and damage these cells. Saccharomyces cerevisiae expressing C. albicans ECM33 did not adhere to or invade epithelial cells, suggesting that Ecm33p by itself does not act as an adhesin or invasin. Examination of ecm33{Delta} mutants by transmission electron microscopy revealed that the cell wall of these strains had an abnormally electron-dense outer mannoprotein layer, which may represent a compensatory response to reduced cell wall integrity. The hyphae of these mutants also had aberrant surface localization of the adhesin Als1p. Collectively, these results suggest that Ecm33p is required for normal cell wall architecture as well as normal function and expression of cell surface proteins in C. albicans.

* Corresponding author. Mailing address: Division of Infectious Diseases, Los Angeles Biomedical Research Institute at Harbor-UCLA Medical Center, 1124 W. Carson St., Torrance, CA 90502. Phone: (310) 222-3813. Fax: (310) 782-2016. E-mail: sfiller{at}ucla.edu.

Eukaryotic Cell, January 2006, p. 140-147, Vol. 5, No. 1
1535-9778/06/$08.00+0     doi:10.1128/EC.5.1.140-147.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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Copyright © 2006 by the American Society for Microbiology.