Antibodies to α5β1 and αvβ3 integrins react with Candida albicans alcohol dehydrogenase

S. A. Klotz, M. L. Pendrak, R. C. Hein

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

It has been hypothesized that Candida albicans possesses integrin-like receptors on its cell surface. This is because C. albicans binds numerous fluid-phase extracellular matrix (ECM) proteins on its cell surface and adheres to the same ECM proteins when immobilized. In addition, numerous antibodies to human integrins (receptors for ECM proteins) bind to the fungal cell surface and in so doing inhibit the binding of the respective proteins. To demonstrate the presence of such a cell surface integrin, a cDNA library of C. albicans yeast cells was screened with polyclonal antiserum to the human fibronectin receptor (α5β1 integrin). Clones isolated by this screening technique also reacted specifically to antiserum against the human vitronectin receptor (αvβ3 integrin). DNA sequence analysis of the cloned insert predicted a 350 aa protein (37 kDa). This predicted protein showed 75% homology at the nucleotide sequence level to alcohol dehydrogenase (ADH) of Saccharomyces cerevisiae. In vitro transcription/translation of the cloned inserts yielded a 37 kDa protein that was immunoprecipated with antibodies to the α5β1 and αvβ3 integrins and an antibody to a C. albicans fibronectin receptor. These antibodies and an mAb to the human vitronectin receptor demonstrated an antigen of -37 kDa present in the cell-wall preparations of C. albicans and in spent growth medium. All four antibodies reacted with authentic ADH. The possible significance of these results in relation to C. albicans adherence is discussed.

Original languageEnglish (US)
Pages (from-to)3159-3164
Number of pages6
JournalMicrobiology
Volume147
Issue number11
DOIs
StatePublished - 2001
Externally publishedYes

Keywords

  • Adherence
  • Candida albicans
  • Extracellular matrix proteins alcohol dehydrogenase
  • Integrins

ASJC Scopus subject areas

  • Microbiology

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