It has been hypothesized that possesses integrin-like receptors on its cell surface. This is because 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 yeast cells was screened with polyclonal antiserum to the human fibronectin receptor (αβ integrin). Clones isolated by this screening technique also reacted specifically to antiserum against the human vitronectin receptor (αβ 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 transcription/translation of the cloned inserts yielded a 37 kDa protein that was immunoprecipated with antibodies to the αβ and αβ integrins and an antibody to a 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 and in spent growth medium. All four antibodies reacted with authentic ADH. The possible significance of these results in relation to adherence is discussed.


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