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.
CITATION STYLE
González, O. G., García, R. M., De La Garza, M., Vaca P., S., Paniagua, G. L., Mejía, R., … Negrete-Abascal, E. (2004). Actinobacillus pleuropneumoniae metalloprotease: Cloning and in vivo expression. FEMS Microbiology Letters, 234(1), 81–86. https://doi.org/10.1016/j.femsle.2004.03.012
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