期刊
LETTERS IN APPLIED MICROBIOLOGY
卷 60, 期 3, 页码 288-297出版社
WILEY
DOI: 10.1111/lam.12373
关键词
AH-3; collagen interaction; cytotoxicity; metalloprotease; microbial collagenase
资金
- European Funds through COMPETE
- National Funds through the Portuguese Science Foundation (FCT) [PEst-C/MAR/LA0017/2013]
- FCT [BPD/38008/2007, BPD/46290/2008, BD/47502/2008]
- Plan Nacional de I+D+I grant (Ministerio de Educacion, Ciencia y Deporte and Ministerio de Sanidad, Spain)
- FIS grant (Ministerio de Educacion, Ciencia y Deporte and Ministerio de Sanidad, Spain)
- Generalitat de Catalunya (Centre de Referencia en Biotecnologia)
The aim of this study was to investigate the presence and the phenotypic expression of a gene coding for a putative collagenase. This gene (AHA_0517) was identified in Aeromonas hydrophila ATCC 7966 genome and named colAh. We constructed and characterized an Aeromonas piscicola AH-3::colAh knockout mutant. Collagenolytic activity of the wild-type and mutant strains was determined, demonstrating that colAh encodes for a collagenase. ColAh-collagen interaction was assayed by Far-Western blot, and cytopathic effects were investigated in Vero cells. We demonstrated that ColAh is a gluzincin metallopeptidase (approx. 100 kDa), able to cleave and physically interact with collagen, that contributes for Aeromonas collagenolytic activity and cytotoxicity. ColAh possess the consensus HEXXH sequence and a glutamic acid as the third zinc binding positioned downstream the HEXXH motif, but has low sequence similarity and distinct domain architecture to the well-known clostridial collagenases. In addition, these results highlight the importance of exploring new microbial collagenases that may have significant relevance for the health and biotechnological industries.
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