Viperidae snakes venoms represent a source of efficient bioactive components that have already led to the development of several new drugs. In this work, we analyzed the protein content of the Montivipera bornmuelleri crude venom using LC-ESI-MS, sephadex G-75 gel filtration and SDS-PAGE and demonstrated the presence of proteins with molecular masses corresponding to metalloprotease III, serine-protease and PLA2 in three fractions collected after gel filtration. Equally, we examined the antimicrobial effect of the venom that showed an important potency, as bactericidal agent, based on MBC and MIC values obtained, against Staphylococcus aureus and Morganella morganii bacteria. However, no activity was registered against Enterococcus faecalis, being the most resistant bacteria, neither against Aspergillus flavus and Penicillium digitatum fungal. Furthermore, on eleven other bacterial strains and the Candida albicans fungus, the venom has shown an intermediate efficacy by slightly reducing the growth. Our data concerning the Montivipera bornmuelleri venom give evidence of a rich and complex content aiding the exploration of new bioactive molecules for biopharmaceuticals purposes.

Viper's venom is a source of biopharmaceutical compounds, hence the need to assess the effect of this animal extract on human blood. Here, we studied the blood coagulation disorders and hemolytic activities of the venom of M. bornmulleri viper. The pro-coagulant and anticoagulant effects are analyzed with venom concentrations ranging from 0.4 to 0.0031 mg/mL. Thus, the PT is way above the normal value indicating an anticoagulant activity whereas for the aPTT, the high concentration of the venom showed an anticoagulant activity, but a pro-coagulant effect was occurred when the venom concentration decreases to 0.05 and/or 0.025 mg/mL. Hemolytic tests, performed in suspension (30% RBCs) and on blood agar plate (5% RBCs), show that an increased concentration of the venom going until 1.6 mg cannot produce a hemolytic effect, even in the presence of Ca 2+ (hemolysis < 0.5%). Also, on the blood agar plate no hemolytic area appeared even with 0.04 mg of the lyophilized venom. Otherwise, the venom was able to induce a low hemolytic activity (hemolysis = 1.3 %) by acting on L-α-PC used as substrate. In this case, the destruction of erythrocytes increased proportionally to the added amount of phospholipids which are hydrolyzed to fatty acids and lysophospholipids (two toxic substances for RBCs), probably due to the presence of PLA2 in the venom and which are known by their ability to hydrolyze lecithin

The L-amino acid oxidase (LAAO) is a multifunctional enzyme, able to partake in different activities including antibacterial activity. In this study, a novel LAAO (Mb-LAAO) was isolated from the venom of M. bornmuelleri snake using size exclusion chromatography followed by RP-HPLC and partially characterized. However, the molecular weight of the Mb-LAAO determined by ESI-MS and SDS-PAGE was 59 960.4 Da. Once the enzymatic activity test confirming the enzyme's identity (transformation of L-leucine) was done, the Mb-LAAO was evaluated for its antibacterial activity against Gram-negative bacteria. It showed a remarkable effect against M. morganii and K. pneumoniae. Moreover, no cytotoxic activity was observed for Mb-LAAO against human erythrocytes arguing for an exploration of its pharmaceutical interest.

No abstract

No abstract