Actinobacillus pleuropneumoniae metalloprotease: cloning and in vivo expression

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 seque...

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Bibliographic Details
Published in:FEMS microbiology letters 2004-05, Vol.234 (1), p.81-86
Main Authors: González, Octavio Garcı́a, Garcı́a, Rosa M., de la Garza, Mireya, P., Sergio Vaca, Luz Paniagua, Gloria, Mejı́a, Ricardo, Tenorio, Vı́ctor R., Negrete-Abascal, Erasmo
Format: Article
Language:English
Subjects:
Actinobacillus pleuropneumoniae
Escherichia coli
Pathogenicity
Porcine pleuropneumonia
Protease
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1016/j.femsle.2004.03.012