Sequencing and characterization of a novel serine metalloprotease from Burkholderia pseudomallei.

Abstract:

:Burkholderia pseudomallei, a Gram-negative bacterium is found in the soil and water, mainly in Southeast Asia and Northern Australia. It is responsible for melioidosis in human and animals. The bacteria produce several potential virulent factors such as extracellular protease, hemolysin, lipase and lecithinase. The isolation of virulence genes and the study of their functions will contribute to our understanding of bacterial pathogenesis. Previous studies have implicated protease as a contributing virulence factor in the pathogenesis of some bacteria. Three out of 5000 clones screened from a genomic DNA library of B. pseudomallei were found to express protease activity. The clones were found to have the same sequence. The nucleotide sequence revealed an open reading frame (designated as metalloprotease A, mprA) encoding a 500-amino acid protein, MprA, with an estimated molecular mass of 50241 Da. The predicted amino acid sequence shares homology with the subtilisin family of serine proteases.

journal_name

FEMS Microbiol Lett

authors

Lee MA,Liu Y

doi

10.1111/j.1574-6968.2000.tb09360.x

keywords:

subject

Has Abstract

pub_date

2000-11-01 00:00:00

pages

67-72

issue

1

eissn

0378-1097

issn

1574-6968

pii

S0378-1097(00)00410-9

journal_volume

192

pub_type

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