Identification and initial characterization of elastase activity associated with Vibrio cholerae.
Strains of Vibrio cholerae O1 (Ogawa, Inaba) and non-O1 serogroups have been found to produce an elastolytic protease that can be detected on 0.3% elastin agar plates or in broth cultures. The elastase enzyme appears to be maximally expressed in late log phase (14-18 h postinoculation) and has optimum activity at a pH range between 7 and 8. Comparative studies indicate that more than 60% of V. cholerae strains analyzed quantitatively produce more elastase in broth (two- to fourfold higher) than other elastase-positive Vibrio species such as Vibrio vulnificus. The V. cholerae elastase enzyme was not inhibited by trypsin, serine-protease, or thiol-protease inhibitors, but was inhibited by phosphoramidon. Ultrafiltration studies indicate the V. cholerae elastase enzyme has a molecular weight >30,000, and a 34K protein with possible elastase activity has been detected by SDS-PAGE for one non-O1 isolate (strain 2396). Cumulative results suggest that the V. cholerae elastase is probably a member of the N-type metalloprotease family and shares similar properties with other elastase enzymes described for pathogenic and nonpathogenic species in this genus.
Janda
J M
JM
Microbial Diseases Laboratory, Division of Communicable Disease Control, California Department of Health Services, 2151 Berkeley Way, Berkeley, CA 94704-1011, USA.
Abbott
S L
SL
Khashe
S
S
D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007700:Kinetics; D010196:Pancreatic Elastase / Q000737:chemistry* / Q000378:metabolism*; D014734:Vibrio cholerae / Q000201:enzymology* / Q000254:growth & development
D010196:Pancreatic Elastase