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Curr Microbiol. 2011 May;62(5):1478-82. doi: 10.1007/s00284-011-9886-4. Epub 2011 Feb 9.

Presence of 46 kDa gelatinase on the outer membrane of Leptospira.

Author information

1
Regional Medical Research Centre (ICMR) and WHO Collaborating Centre for Diagnosis, Reference, Research and, Training in Leptospirosis, Post Bag No. 13, Port Blair 744 101, Andaman and Nicobar Islands, India. madananmg@icmr.org.in

Abstract

Leptospira infection involves the adhesion of the bacteria followed by invasion of the host crossing the extracellular matrix barrier. In an effort to understand the molecular mechanism of this process, the possibility of occurrence of matrix degrading enzymes from Leptospira was investigated. Zymographic analysis showed that the outer membrane of Leptospires contains a gelatinase of average molecular size of 46 kDa. The gelatinase exhibited maximum activity at neutral pH and was inhibited by metal chelators such as EGTA, EDTA, and Orthophenanthroline and was activated by calcium, magnesium, zinc, and copper, suggesting that it is a membrane-associated neutral matrix metalloproteinase. Analysis of the production of the enzyme by various serovars showed that the pathogenic serovars expressed significant amount of this enzyme while nonpathogenic forms either did not express or showed only very low activity, suggesting that this enzyme may be associated with pathogenesis of leptospirosis.

PMID:
21305291
DOI:
10.1007/s00284-011-9886-4
[Indexed for MEDLINE]

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