K. Cavedon et J. London, ADHESION DEGRADATION - A POSSIBLE FUNCTION FOR A PREVOTELLA-LOESCHEIIPROTEASE, Oral microbiology and immunology, 8(5), 1993, pp. 283-287
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.