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Memórias do Instituto Oswaldo Cruz
Fundação Oswaldo Cruz, Fiocruz
ISSN: 1678-8060
EISSN: 1678-8060
Vol. 104, No. 8, 2009, pp. 1132-1138
Bioline Code: oc09228
Full paper language: English
Document type: Research Article
Document available free of charge

Memórias do Instituto Oswaldo Cruz, Vol. 104, No. 8, 2009, pp. 1132-1138

 en Cloning, expression and characterisation of an HtrA-like serine protease produced in vivo by Mycobacterium leprae check for this species in other resources
Ribeiro-Guimarães, Michelle Lopes; Marengo, Eliana Blini; Tempone, Antonio Jorge; Amaral, Julio Jablonski; Klitzke, Clécio F; da Silveira, Erika K Xavier; Portaro, Fernanda Calheta Vieira & Pessolani, Maria Cristina Vidal

Abstract

Members of the high temperature requirement A (HtrA) family of chaperone proteases have been shown to play a role in bacterial pathogenesis. In a recent report, we demonstrated that the gene ML0176, which codes for a predicted HtrA-like protease, a gene conserved in other species of mycobacteria, is transcribed by Mycobacterium leprae check for this species in other resources in human leprosy lesions. In the present study, the recombinant ML0176 protein was produced and its enzymatic properties investigated. M. leprae recombinant ML0176 was able to hydrolyse a variety of synthetic and natural peptides. Similar to other HtrA proteins, this enzyme displayed maximum proteolytic activity at temperatures above 40°C and was completely inactivated by aprotinin, a protease inhibitor with high selectivity for serine proteases. Finally, analysis of M. leprae ML0176 specificity suggested a broader cleavage preference than that of previously described HtrAs homologues. In summary, we have identified an HtrA-like protease in M. leprae that may constitute a potential new target for the development of novel prophylactic and/or therapeutic strategies against mycobacterial infections.

Keywords
Mycobacterium leprae - HtrA2 - protease - enzymatic activity - FRET peptides - pathogenesis

 
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