Effects of snake venom proteases on human fibrinogen chains.

Abstract

Proteomic approach is an effective method to study changes in human plasma proteome. Coagulopathies are commonly encountered in victims of viper envenomation which were treated with an administration of immunoglobulin. Unfortunately, this treatment shows significant risk to the patient due to an anaphylactic reaction. Since Echis carinatus Venom (EV) toxins mainly acts both directly and indirectly on fibrinogen, we planned to establish a suitable analysis of its beta (FIBB) e gamma (FIBG) chains. This study will help us to understand the mechanism of envenomation and to find alternative treatments other than the common treatment with the administration of IgG. We evaluated the EV proteolytic activity on whole human plasma proteome from the blood of an healthy volunteer. Two-dimensional electrophoresis (2-DE) using mini-gel was performed to analyse EV effects on the differents fibrinogen chains. Changes in whole plasma proteome were focused on fibrinogen beta and gamma chains after EV incubation. Protein spots were detected and analyzed using ImageMaster 2D Platinum software. Results were represented as mean +/- standard deviation (mean+/-SD) with p<0.05 as a statistically significant value. 2-DE gel analysis showed that some spots of FIBB disappeared and some spots of FIBG decreased. We found that the proteomic approach is a valid method in studying in-depth causes of different diseases, in particular those are involved in coagulopathies linked with proteins like fibrinogen from victims of viper envenomation.