Actinobacillus pleuropneumoniae metalloprotease: Cloning and in vivo expression

  • O.G. G
  • R.M. G
  • M. D
  • et al.
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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.




O.G., G., R.M., G., M., D. L. G., S., V. P., G.L., P., R., M., & V.R., T. (2004). Actinobacillus pleuropneumoniae metalloprotease: Cloning and in vivo expression. FEMS Microbiology Letters. E. Negrete-Abascal, Carrera de Biologia, Fac. de Estudios Superiores Iztacala, UNAM, Av. de los Barrios #1, Estado de Mexico 54090, Mexico. E-mail: Elsevier. Retrieved from

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