Using ELISA assays we established a high correlation between the protective efficacy of the whole venom antisera in mice and their anti-Atxs antibody content. As the haemorrhage is the prevailing toxic effect of the venom in human, the lack of correlation also with anti-H IgG content exposed that the mouse model might not be optimal to evaluate the neutralizing potential of the venom-specific antisera for human therapy. We further revealed that Atxs and structurally very similar but non-toxic AtnI2 from the venom are not immuno cross-reactive.
COBISS.SI-ID: 21825831
Here we report on purification and characterization of two activators of coagulation factor X (FX), 58 kDa VAFXA-I and 70 kDa VAFXA-II from Vipera a. ammodytes venom. The VAFXAs activate FX in a Ca2+-dependent manner with the same specificity as physiological activators. The activators did not activate prothrombin or plasminogen but inhibit collagen-induced platelet aggregation in vitro. They activate coagulation FX to FXa without toxic effects. Their application in treating patients with dysfunctional factors IXa or VIIa to restore the normal blood coagulation process is thus promising.
COBISS.SI-ID: 21894439
Ammodytoxin A (AtxA) and its natural isoform AtxC from the venom of Vipera a. ammodytes exhibit strong neurotoxic and anticoagulant effects. The two isoforms, which differ in sequence by only two amino acid residues, display significant differences in toxicity and anticoagulant properties and act on protein targets including neurotoxic proteic receptors and coagulation factor Xa with significantly different strengths of binding. In this work we determined the three-dimensional structure of both molecules and by their comparison explained the pharmacological differences between both Atxs.
COBISS.SI-ID: 23047975
In this work we demonstrated intraspecific variability between 8 Vipera a. ammodytes venom production batches. For the first time we were able to select those biochemical differences that are related to and give information on the venom's toxicity and immunogenicity. We have shown that methods quantifying ammodytoxin (the most toxic compound identified so far in the Vipera a. ammodytes venom) content of the venom clearly distinguish between high and low immunogenic venoms.
COBISS.SI-ID: 24083495
In this invited review we descride the most relevant haemostatically active proteins from snake venoms. Medical applications have already been found for some of these snake venom proteins. We describe those that have already been approved as drugs to treat haemostatic disorders or are being used to diagnose such health problems. No clinical applications, however, currently exist for the majority of snake venom proteins acting on haemostasis. We conclude with the most promising potential uses in this respect.
COBISS.SI-ID: 24433959