title: Characterization of a human chorionic gonadotropin-like protein from Candida albicans.
abstract: Studies from our laboratory have demonstrated that human CG (hCG), human LH, (hLH), and an hCG-like protein extracted from Xanthomonas maltophilia were able to induce Candida albicans transition from the blastospore to the germ tube stage. In the present study, we describe the characterization of an hCG-like material extracted from Candida albicans blastospores (CaCGLP), which is potent in inducing transition and presumably represents the endogenous transition-inducing substance. This material was extracted from Candida albicans blastospores with glacial acetic acid and purified by affinity chromatography using a polyclonal rabbit anti-hCG antibody. The product obtained is a 68-kilodalton single band protein, as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analysis. Under reduced conditions a protein smear is seen. Amino acid analysis showed a predominance of glycine (22%), followed by serine (12%), and glutamate (12%). This protein reacted in the following hCG immunoassays: 1) a polyclonal rabbit anti-hCG equilibrium assay, 2) a carboxyl-tail hCG equilibrium assay, 3) two hCG equilibrium assays using monoclonal antibodies (CG no. 4 and CG no. 9), 4) a free alpha-subunit equilibrium assay using a monoclonal antibody, and 5) an ultrasensitive immunoradiometric assay for hCG which does not cross-react with hLH, nor the free beta-subunit of hCG. The CaCGLP showed no reaction in a specific hLH immunoradiometric assay. When CaCGLP was tested in the transition assay, in the presence of 4% rat serum, it was found that this protein was 100 times more potent than hCG in producing Candida albicans transition. We conclude that Candida albicans produces a protein that has certain tertiary structure similarities to hCG and that this material is able to induce germ tube formation. We postulate that CaCGLP has an autocrine/paracrine effect in Candida albicans as a transition factor to control its own pathogenicity.
authors.affiliation: Department of Internal Medicine, University of Utah School of Medicine, Salt Lake City 84132.
authors.forename: O
authors.initials: O
authors.lastname: Caticha
authors.forename: Y
authors.initials: Y
authors.lastname: Li
authors.forename: J
authors.initials: J
authors.lastname: Griffin
authors.forename: D
authors.initials: D
authors.lastname: Winge
authors.forename: W D
authors.initials: WD
authors.lastname: Odell
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000911:Antibodies, Monoclonal; D015153:Blotting, Western; D002176:Candida albicans / Q000737:chemistry* / Q000187:drug effects / Q000201:enzymology; D006063:Chorionic Gonadotropin / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007118:Immunoassay; D008970:Molecular Weight; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013172:Spores, Fungal / Q000737:chemistry / Q000201:enzymology
chemical_list: D000596:Amino Acids; D000911:Antibodies, Monoclonal; D006063:Chorionic Gonadotropin; D011506:Proteins; D010450:Endopeptidases