Open AccessSequencing and characterization of a novel serine metalloprotease from Burkholderia pseudomallei
Author(s) -
Lee MayAnn,
Liu Yichun
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09360.x
Subject(s) - burkholderia pseudomallei , biology , microbiology and biotechnology , proteases , virulence , serine protease , burkholderia , peptide sequence , protease , open reading frame , nucleic acid sequence , tmprss6 , hemolysin , lecithinase , bacteria , genetics , gene , biochemistry , enzyme
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 50 241 Da. The predicted amino acid sequence shares homology with the subtilisin family of serine proteases.