Degenerate Peptide Recognition by Candida albicans Adhesins Als5p and Als1p

Stephen A Klotz, Nand K. Gaur, Douglas F. Lake, Vincent Chan, Jason Rauceo, Peter N. Lipke

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

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 96-μm-diameter polyethylene glycol beads coated with a 7-mer peptide from a library of 19 7 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 (τψ+) 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.

Original languageEnglish (US)
Pages (from-to)2029-2034
Number of pages6
JournalInfection and Immunity
Volume72
Issue number4
DOIs
StatePublished - Apr 2004

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Peptides
Saccharomyces cerevisiae
Candida albicans
Adhesives
Amino Acid Sequence
Candida albicans ALA1 protein
Immobilized Proteins
Peptide Library
Amino Acid Motifs
Proteins
Protein Sequence Analysis
Libraries
Fungi
Yeasts
Phenotype

ASJC Scopus subject areas

  • Immunology

Cite this

Degenerate Peptide Recognition by Candida albicans Adhesins Als5p and Als1p. / Klotz, Stephen A; Gaur, Nand K.; Lake, Douglas F.; Chan, Vincent; Rauceo, Jason; Lipke, Peter N.

In: Infection and Immunity, Vol. 72, No. 4, 04.2004, p. 2029-2034.

Research output: Contribution to journalArticle

Klotz, Stephen A ; Gaur, Nand K. ; Lake, Douglas F. ; Chan, Vincent ; Rauceo, Jason ; Lipke, Peter N. / Degenerate Peptide Recognition by Candida albicans Adhesins Als5p and Als1p. In: Infection and Immunity. 2004 ; Vol. 72, No. 4. pp. 2029-2034.
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