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Infection and Immunity, September 2004, p. 4948-4955, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.4948-4955.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Global Cell Surface Conformational Shift Mediated by a Candida albicans Adhesin

Jason M. Rauceo,1 Nand K. Gaur,2 Kyeng-Gea Lee,1 John E. Edwards,3 Stephen A. Klotz,2,4 and Peter N. Lipke1*

Department of Biological Sciences and the Center for Gene Structure and Function, Hunter College of the City University of New York, New York, New York,1 Southern Arizona Veterans Administration Health Care System,2 Department of Medicine, University of Arizona, Tucson, Arizona,4 Harbor-UCLA Research and Education Institute, Torrance, California3

Received 23 January 2004/ Returned for modification 5 February 2004/ Accepted 14 May 2004

Candida albicans maintains both commensal and pathogenic states in humans. Both states are dependent on cell surface-expressed adhesins, including those of the Als family. Heterologous expression of Als5p at the surface of Saccharomyces cerevisiae results in Als5p-mediated adhesion to various ligands, followed by formation of multicellular aggregates. Following adhesion of one region of the cell to fibronectin-coated beads, the entire surface of the cells became competent to mediate cell-cell aggregation. Aggregates formed in the presence of metabolic inhibitors or signal transduction inhibitors but were reduced in the presence of 8-anilino-1-naphthalene-sulfonic acid (ANS) or Congo Red (CR), perturbants that inhibit protein structural transitions. These perturbants also inhibited aggregation of C. albicans. An increase in ANS fluorescence, which accompanied Als-dependent cellular adhesion, indicated an increase in cell surface hydrophobicity. In addition, C. albicans and Als5p-expressing S. cerevisiae showed an aggregation-induced birefringence indicative of order on the cell surface. The increase in birefringence did not occur in the presence of the aggregation disruptants ANS and CR. These results suggest a model for Als5p-mediated aggregation in which an adhesion-triggered change in the conformation of Als5p propagates around the cell surface, forming ordered aggregation-competent regions.

* Corresponding author. Mailing address: Department of Biology, Hunter College, 695 Park Ave., New York, NY 10021. Phone: (212) 772-5235. Fax: (212) 772-5227. E-mail: lipke{at}genectr.hunter.cuny.edu.

Editor: T. R. Kozel

Infection and Immunity, September 2004, p. 4948-4955, Vol. 72, No. 9
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.9.4948-4955.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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