title: Scanning electron microscopy of epidermal adherence and cavitation in murine candidiasis: a role for Candida acid proteinase.
abstract: Adherence of blastoconidia to epidermal corneocytes is an early event in Candida colonization and infection of the skin. Pathogenic species adhere more avidly than nonpathogenic species, transform to hyphal growth, and invade the stratum corneum of the skin. Adherence was studied by scanning electron microscopy of experimental murine cutaneous Candida infections, using six species of Candida. Candida albicans and C. stellatoidea blastoconidia, applied to newborn mouse skin, adhered to the stratum corneum in greater numbers than other species tested, acquired fibrils and strands of amorphous mucinlike material ("cohesin") between spores and the corneocyte cell surface, formed cavitations in the corneocyte surface, and invaded the corneocyte envelope by hyphal growth at sites distant to the point of blastoconidia attachment. Other species showed little or no adherence, colonization, or cavitation of the corneocyte surface, except C. tropicalis, which showed intermediate results. Pepstatin, an inhibitor of Candida acid proteinase, did not alter adherence or cohesion formation, but inhibited formation of corneocyte cavitations about adherent blastoconidia, suggesting that this enzyme may facilitate adherence/invasion events on skin. Depletion of surface lipids did not alter the formation of cohesin material or the adherence process. Adherence and invasion of epithelium by pathogenic Candida species include the interaction of blastoconidia with an epithelial surface cohesin material that participates in the adherence process. Candida acid proteinase, a keratinolytic enzyme, may participate in the cavitation process of the corneocyte surface by C. albicans.
authors.affiliation: Marshall Dermatology Research Laboratories, Department of Dermatology, University of Iowa College of Medicine, Iowa City 52242.
authors.forename: T L
authors.initials: TL
authors.lastname: Ray
authors.forename: C D
authors.initials: CD
authors.lastname: Payne
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002175:Candida / Q000201:enzymology / Q000472:pathogenicity*; D002177:Candidiasis / Q000473:pathology*; D002448:Cell Adhesion; D010450:Endopeptidases / Q000502:physiology*; D004817:Epidermis / Q000382:microbiology / Q000473:pathology; D051379:Mice; D008855:Microscopy, Electron, Scanning; D010436:Pepstatins / Q000494:pharmacology; D013997:Time Factors
chemical_list: D010436:Pepstatins; C014195:Streptomyces pepsin inhibitor; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C031375:pepstatin