2008
DOI: 10.1139/w07-109
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Pathogenic potential of a collagenase gene fromAeromonas veronii

Abstract: The role of collagenase as a mechanism of bacterial pathogenicity in some pathogenic bacteria has been reported. The information on the role of collagenase in Aeromonas spp. pathogenesis is scant. In the present study, a mutant Aeromonas veronii RY001 that is deficient in the putative collagenase gene acg was constructed and compared with the wild-type strain for virulence factors. Bacterial cells and cell-free extracellular products of the mutant had significantly less collagenolytic activity, but there were … Show more

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Cited by 40 publications
(35 citation statements)
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“…ECPs, such as collagenase were reported as the important virulent factor to A. veroni bv. veronii (7). In the present study, the ECPs of strain PY50 was lethal to Chinese longsnout catfish and the LD 50 was 11.22 g per fish, and the results were in accordance with the above-mentioned study.…”
Section: Evaluation Of Putative Virulence Factorssupporting
confidence: 92%
“…ECPs, such as collagenase were reported as the important virulent factor to A. veroni bv. veronii (7). In the present study, the ECPs of strain PY50 was lethal to Chinese longsnout catfish and the LD 50 was 11.22 g per fish, and the results were in accordance with the above-mentioned study.…”
Section: Evaluation Of Putative Virulence Factorssupporting
confidence: 92%
“…Several factors probably play important roles in this process, in addition to adhesive factors needed for step 1 that are listed under gastroenteritis. Aeromonas species elaborate a wide range of microbial proteases (metalloproteases, serine proteases, and aminopeptidases) capable of degrading complex biologic proteins present in serum and connective tissue, including albumin, fibrinogen, elastin, and collagen (107,132,136,137). Degradation of such tissues and proteins can serve as an energy source for subsequent multiplication.…”
Section: Organotrophic Diseasementioning
confidence: 99%
“…Protease PrtC from Porphyromonas gingivalis ATCC 53977 (which is no longer available from the ATCC) was the first reported and is also the most studied U32 protease (78). The other members of this family are from Helicobacter pylori, Salmonella enterica serovar Typhimurium, Clostridium beijerinckii, Escherichia coli, and Bacillus subtilis (79)(80)(81)(82). The prtC gene from Porphyromonas gingivalis ATCC 53977 contains 1,002 bp and encodes a 333-residue PrtC protein (78).…”
Section: Bacterial Collagenolytic Proteases From the U32 Familymentioning
confidence: 99%