ADHESION DEGRADATION - A POSSIBLE FUNCTION FOR A PREVOTELLA-LOESCHEIIPROTEASE

Citation
K. Cavedon et J. London, ADHESION DEGRADATION - A POSSIBLE FUNCTION FOR A PREVOTELLA-LOESCHEIIPROTEASE, Oral microbiology and immunology, 8(5), 1993, pp. 283-287
Citations number
18
Categorie Soggetti
Immunology,Microbiology
ISSN journal
09020055
Volume
8
Issue
5
Year of publication
1993
Pages
283 - 287
Database
ISI
SICI code
0902-0055(1993)8:5<283:AD-APF>2.0.ZU;2-Q
Abstract
Prevotella loescheii PK1295 produces at least 3 proteases that are sep arable 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 fim bria-associated adhesin on P loescheii responsible for coaggregation w ith Streptococcus oralis 34, as well as gelatin, casein and fibrin. Th e action of this protease may contribute to the detachment of P. loesc heii from its streptococcal coaggregation partner and provide a mechan ism for bacterial relocation in dental plaque.