title: Antibodies to alpha5beta1 and alpha(v)beta3 integrins react with Candida albicans alcohol dehydrogenase.
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 (alpha5beta1 integrin). Clones isolated by this screening technique also reacted specifically to antiserum against the human vitronectin receptor (alpha(v)beta3 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 immunoprecipitated with antibodies to the alpha5beta1 and alpha(v)beta3 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.
authors.affiliation: Research Service, Southern Arizona Veterans Affairs Health Service System, Tucson, AZ, USA. sklotz@u.arizona.edu
authors.forename: S A
authors.initials: SA
authors.lastname: Klotz
authors.forename: M L
authors.initials: ML
authors.lastname: Pendrak
authors.forename: R C
authors.initials: RC
authors.lastname: Hein
mesh_terms: D000426:Alcohol Dehydrogenase / Q000235:genetics / Q000276:immunology*; D000907:Antibodies, Bacterial / Q000276:immunology*; D000911:Antibodies, Monoclonal / Q000276:immunology; D002176:Candida albicans / Q000201:enzymology* / Q000276:immunology* / Q000378:metabolism / Q000648:ultrastructure; D002448:Cell Adhesion; D002473:Cell Wall / Q000502:physiology; D003001:Cloning, Molecular; D003429:Cross Reactions; D004926:Escherichia coli; D015723:Gene Library; D006801:Humans; D011485:Protein Binding; D016024:Receptors, Cytoadhesin / Q000032:analysis / Q000378:metabolism; D017469:Receptors, Fibronectin / Q000276:immunology*; D019030:Receptors, Vitronectin / Q000276:immunology*; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000502:physiology
chemical_list: D000907:Antibodies, Bacterial; D000911:Antibodies, Monoclonal; D016024:Receptors, Cytoadhesin; D017469:Receptors, Fibronectin; D019030:Receptors, Vitronectin; D000426:Alcohol Dehydrogenase