Proteolytic activity in black-pigmented bacteroides species.
Black-pigmented Bacteroides species are frequently found in dentoalveolar abscesses. One general mechanism of bacterial virulence is the production of extracellular enzymes which degrade connective tissue or molecules associated with host defense. In this study the proteolytic activity of 18 bacterial strains from 9 black-pigmented Bacteroides species was examined. Bacteroides gingivalis degraded the greatest number of substrates studied and produced the highest levels of enzymatic activity. B. gingivalis was the only species that degraded collagen and produced high levels of enzymes that degraded N-benzoyl-DL-arginine (BANA) and N-CBz-glycyl-glycyl-arginine. Bacteroides intermedius degraded several substrates including PZ peptide. Bacteroides endodontalis produced enzymes that degraded beta-naphthylamide derivatives of glycylproline and glycylphenylalanine. There were considerable differences in enzyme production between strains of the same species. Such heterogeneity between strains in the production of proteolytic enzymes may be relevant to the in vivo infections produced in the host.
Jun
K C
KC
Barua
P K
PK
Zambon
J J
JJ
Neiders
M E
ME
D001391:Azo Compounds / Q000378:metabolism; D001439:Bacteroides / Q000201:enzymology*; D003094:Collagen / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D008666:Metalloendopeptidases; D003012:Microbial Collagenase / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D001443:Prevotella melaninogenica / Q000201:enzymology
D001391:Azo Compounds; D009842:Oligopeptides; C043091:PZ-peptide; C028470:Azocoll; D003094:Collagen; D010450:Endopeptidases; D010447:Peptide Hydrolases; D008666:Metalloendopeptidases; C022510:thimet oligopeptidase; D003012:Microbial Collagenase