Actinobacillus pleuropneumoniae metalloprotease: Cloning and in vivo expression

  • González O
  • García R
  • De La Garza M
 et al. 
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Abstract

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. © 2004 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.

Author-supplied keywords

  • Escherichia coli
  • Pathogenicity
  • Porcine pleuropneumonia
  • Protease

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Authors

  • Octavio García González

  • Rosa M. García

  • Mireya De La Garza

  • Sergio Vaca P.

  • Gloria Luz Paniagua

  • Ricardo Mejía

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