Open AccessActinobacillus pleuropneumoniae metalloprotease: cloning and in vivo expression
Author(s) -
O GONZALEZ
Publication year - 2004
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 - 10.1016/j.femsle.2004.03.012
Subject(s) - actinobacillus pleuropneumoniae , biology , peptide sequence , metalloproteinase , nucleic acid sequence , aminopeptidase , microbiology and biotechnology , protease , open reading frame , actinobacillus , clone (java method) , gene , amino acid , serotype , bacteria , biochemistry , genetics , enzyme , leucine
The complete amino acid and nucleotide sequence of a secreted metalloprotease produced by Actinobacillus pleuropneumoniae serotype 1 is reported. A clone showing proteolytic activity in cell-free culture media was selected from a genomic library of A. pleuropneumoniae serotype 1 in pUC 19. The sequence obtained contained an open reading frame encoding a protein with 869 amino acids. This protein was identified as a zinc neutral-metalloprotease belonging to the aminopeptidase family, with a predicted molecular weight of approximately 101 kDa. This sequence showed high homology with other predicted or sequenced aminopeptidases reported for different Gram-negative bacteria. Expression of the protease was observed in lung tissue from pigs that died of porcine pleuropneumonia suggesting a role in pathogenesis.
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