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Infection and Immunity, April 2004, p. 2029-2034, Vol. 72, No. 4
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.4.2029-2034.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Degenerate Peptide Recognition by Candida albicans Adhesins Als5p and Als1p

Stephen A. Klotz,1,2* Nand K. Gaur,2 Douglas F. Lake,3 Vincent Chan,2 Jason Rauceo,4 and Peter N. Lipke4

Department of Medicine, University of Arizona,1 Southern Arizona VA Health Care System,2 Arizona Cancer Center, Tucson, Arizona 55724,3 Department of Biological Sciences and Center for Gene Structure and Function, Hunter College of the City University of New York, New York, New York 100214

Received 29 October 2003/ Returned for modification 19 November 2003/ Accepted 12 December 2003

Candida albicans and Saccharomyces cerevisiae expressing the adhesins Als5p or Als1p adhere to immobilized peptides and proteins that possess appropriate sequences of amino acids in addition to a sterically accessible peptide backbone. In an attempt to further define the nature of these targets, we surveyed the ability of yeast cells to adhere to 90-µm-diameter polyethylene glycol beads coated with a 7-mer peptide from a library of 197 unique peptide-beads. C. albicans bound to ca. 10% of beads from the library, whereas S. cerevisiae expressing Als5p or Als1p bound to ca. 0.1 to 1% of randomly selected peptide-beads. S. cerevisiae expressing Als1p had a distinctly different adherence phenotype than did cells expressing Als5p. The former adhered in groups or clumps of cells, whereas the latter adhered initially as single cells, an event which was followed by the build up of cell-cell aggregates. Beads with adherent cells were removed, and the peptide attached to the bead was determined by amino acid sequencing. All adhesive beads carried a three-amino-acid sequence motif ({tau}{varphi}+) that possessed a vast combinatorial potential. Adherence was sequence specific and was inhibited when soluble peptide identical to the immobilized peptide was added. The Als5p adhesin recognized some peptides that went unrecognized by Als1p. The sequence motif of adhesive peptides identified by this method is common in proteins and offers so many possible sequence combinations that target recognition by the Als proteins is clearly degenerate. A degenerate recognition system provides the fungi with the potential of adhering to a multitude of proteins and peptides, an advantage for any microorganism attempting to establish a commensal or pathogenic relationship with a host.

* Corresponding author. Mailing address: Section of Infectious Diseases, University of Arizona Health Sciences Center, 1501 N. Campbell, Tucson, AZ 85724. Phone: (520) 626-6887. Fax: (520) 626-5183. E-mail: sklotz{at}u.arizona.edu.

Editor: T. R. Kozel

Infection and Immunity, April 2004, p. 2029-2034, Vol. 72, No. 4
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.4.2029-2034.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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