Adhesive and Mammalian Transglutaminase Substrate Properties of Candida albicans Hwp1
- 5 March 1999
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 283 (5407) , 1535-1538
- https://doi.org/10.1126/science.283.5407.1535
Abstract
The pathogenesis of candidiasis involves invasion of host tissues by filamentous forms of the opportunistic yeast Candida albicans. Morphology-specific gene products may confer proinvasive properties. A hypha-specific surface protein, Hwp1, with similarities to mammalian small proline-rich proteins was shown to serve as a substrate for mammalian transglutaminases. Candida albicansstrains lacking Hwp1 were unable to form stable attachments to human buccal epithelial cells and had a reduced capacity to cause systemic candidiasis in mice. This represents a paradigm for microbial adhesion that implicates essential host enzymes.Keywords
This publication has 19 references indexed in Scilit:
- Developmental Expression of a Tandemly Repeated, Proline- and Glutamine-rich Amino Acid Motif on Hyphal Surfaces of Candida albicansJournal of Biological Chemistry, 1996
- Cloning and Regulation of Cornifin β, a New Member of the Cornifin/spr FamilyPublished by Elsevier ,1996
- Use of Percoll Density Gradients for Studying the Attachment of Bacteria to Oral Epithelial CellsJournal of Dental Research, 1988
- Transamidating activities of factor XIIIa and of transglutaminases, measured by an Elisa procedureBiochemical and Biophysical Research Communications, 1988
- [46] TransglutaminasesPublished by Elsevier ,1985
- Fluorographic detection of radioactivity in polyacrylamide gols with the water-soluble fluor, sodium salicylateAnalytical Biochemistry, 1979
- Acetylglucagon: Preparation and CharacterizationEuropean Journal of Biochemistry, 1975
- A filter paper assay for transamidating enzymes using radioactive amine substratesAnalytical Biochemistry, 1972
- Transamidating enzymesAnalytical Biochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970