title: Adhesin degradation: a possible function for a Prevotella loescheii protease?
abstract: Prevotella loescheii PK1295 produces at least 3 proteases that are separable by isoelectric focusing. One of these proteases, an enzyme with an isoelectric point at 8.5 and an M(r) of 36,000, hydrolyzes the fimbria-associated adhesin on P. loescheii responsible for coaggregation with Streptococcus oralis 34, as well as gelatin, casein and fibrin. The action of this protease may contribute to the detachment of P. loescheii from its streptococcal coaggregation partner and provide a mechanism for bacterial relocation in dental plaque.
authors.affiliation: Laboratory of Microbial Ecology, National Institute of Dental Research, US National Institutes of Health, Bethesda, Maryland.
authors.forename: K
authors.initials: K
authors.lastname: Cavedon
authors.forename: J
authors.initials: J
authors.lastname: London
mesh_terms: D018829:Adhesins, Bacterial; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D001439:Bacteroides / Q000201:enzymology*; D003773:Dental Plaque / Q000382:microbiology; D004591:Electrophoresis, Polyacrylamide Gel; D010861:Fimbriae, Bacterial; D007525:Isoelectric Focusing; D010447:Peptide Hydrolases / Q000378:metabolism
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; C063910:adhesin, Bacteroides; D010447:Peptide Hydrolases