SYSTEM OF ACTIVATION OF PLASMINOGEN IN VIBRIO CHOLERAE

Aim. Study system of activation of plasminogen in Vibrio cholerae. Materials and methods. 75 strains of V. cholerae of various origins were used in the study. Plasminogen was isolated from human plasma by using affinity chromatography on L-lysine sepharose, α-enolase activity was determined by a direct method assuming transformation of 2-phosphoglycerate into phopshoenolpyruvate. Vibrios were destroyed by ultrasound disintegrator to isolate membrane OmpT protein, intact cells were discarded by centrifugation and cell lysate was centrifugated for 1 hour at 105000 g. The precipitate was solubilized in buffer with 1% triton X-100 and passed through a column with DE-52 cellulose. Results. Vibrio cholerae O1 and O139 strains isolated from clinical specimens and water samples from open water bodies had the ability to bind by using α-enolase and transform human plasminogen into plasmin under the effect ofouter membrane protein OmpT. A protein with molecular weight around 40 kDa had proteolytic activity with a wide specter of substrate specificity, degraded fibrin, gelatin, collagen, protamine and activated plasminogen. Computer analysis showed that OmpT protein of cholera vibrion had a low degree of relation with Enterobacteriaceae omptins. Conclusion. The study carried out showed that vibrios have a system of activation of plasminogen that includes at least α-enolase and OmpT membrane protein. OmpT protein is assumed to belong to a new class of porins of Vibrionaceae family and its enzymatic activity may play a significant role in pathogenesis of infection.

plasmin, plasminogen, α-enolase, strains, vibrios, omptins, porins