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.
Microbial Diseases Laboratory, Division of Communicable Disease Control, California Department of Health Services, 2151 Berkeley Way, Berkeley, CA 94704-1011, USA.
J M
JM
Janda
S L
SL
Abbott
S
S
Khashe
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