ArticleJournal of bacteriology2009
The AsaP1 peptidase of Aeromonas salmonicida subsp. achromogenes is a highly conserved deuterolysin metalloprotease (family M35) and a major virulence factor.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Evolutionary History and Diversification of M35 Metalloproteases in Dothideomycetes: A Phylogenomic Overview and Case Study in Corynespora cassiicola.Current microbiology · 2026Article
- Zinc metalloprotease FgM35, which targets the wheat zinc-binding protein TaZnBP, contributes to the virulence of Fusarium graminearum.Stress biology · 2024Article
- A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond.Virulence · 2020Article
- Genome-Wide Identification of M35 Family Metalloproteases inInternational journal of molecular sciences · 2020Article
- Characterization of Heterobasidion occidentale transcriptomes reveals candidate genes and DNA polymorphisms for virulence variations.Microbial biotechnology · 2018Article
- Article
- Combining quantitative genetic footprinting and trait enrichment analysis to identify fitness determinants of a bacterial pathogen.PLoS genetics · 2013Article
- Influence of temperature during crystallization setup on precipitate formation and crystal shape of a metalloendopeptidase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Crystallization and preliminary X-ray diffraction studies of AsaP1_E294A and AsaP1_E294Q, two inactive mutants of the toxic zinc metallopeptidase AsaP1 from Aeromonas salmonicida subsp. achromogenes.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
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6 authors.
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Abstract
Infections by the bacterium Aeromonas salmonicida subsp. achromogenes cause significant disease in a number of fish species. In this study, we showed that AsaP1, a toxic 19-kDa metallopeptidase produced by A. salmonicida subsp. achromogenes, belongs to the group of extracellular peptidases (Aeromonas type) (MEROPS ID M35.003) of the deuterolysin family of zinc-dependent aspzincin endopeptidases. The structural gene of AsaP1 was sequenced and found to be highly conserved among gram-negative bacteria. An isogenic Delta asaP1 A. salmonicida subsp. achromogenes strain was constructed, and its ability to infect fish was compared with that of the wild-type (wt) strain. The Delta asaP1 strain was found to infect Arctic charr, Atlantic salmon, and Atlantic cod, but its virulence was decreased relative to that of the wt strain. The 50% lethal dose of the AsaP1 mutant was 10-fold higher in charr and 5-fold higher in salmon than that of the wt strain. The pathology induced by the AsaP1-deficient strain was also different from that of the wt strain. Furthermore, the mutant established significant bacterial colonization in all observed organs without any signs of a host response in the infected tissue. AsaP1 is therefore the first member of the M35 family that has been shown to be a bacterial virulence factor.
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