1P019 Crystal structure of the serine protease from Aeromonas sobria

Aeromonas sobria Released from Production of C5a by ASP, a Serine Protease

Impaired plasma clottability induction through fibrinogen degradation by ASP, a serine protease released from Aeromonas sobria

Aeromonas sobria infection often advances to sepsis, in which interaction of bacterial components with plasma proteins possibly causes various disorders. This bacterium releases a serine protease (ASP), a putative virulence factor, and binds to fibrinogen. To study the ASP effect on fibrinogen, we incubated fibrinogen or plasma with ASP and investigated their clotting elicited by thrombin, whic...

Involvement of the Arg566 residue of Aeromonas sobria serine protease in substrate specificity

Aeromonas sobria serine protease (ASP) is an extracellular serine protease secreted by the organism. Here, we identified the amino acid residue of ASP that contributes to substrate specificity by using both synthetic peptides and biological protein components. The results showed that the arginine residue at position 566 (Arg-566) of ASP, which is located in the extra occluding region of ASP clo...

Aeromonas sobria a Serine Proteinase from Pressure Lowering through Kinin Release by Induction of Vascular Leakage and Blood

In vitro susceptibilities of Aeromonas hydrophila, Aeromonas sobria, and Aeromonas caviae to 22 antimicrobial agents.

MICs of 22 antimicrobial agents for 60 strains of three Aeromonas species were determined by a microdilution method. The newer cephalosporins such as moxalactam, cefotaxime, and cefoperazone, the aminoglycosides, and chloramphenicol, tetracycline, nitrofurantoin, and trimethoprim-sulfamethoxazole inhibited most of the strains studied. Within the genus, A. hydrophila was more resistant than eith...