1.

Characterization of a novel herorrganic metalloprotease from the venom of the long-nosed viper, Vipera ammodytes ammodytes.

We purified potently hemorrhagic VaH3 from the the long-nosed viper venom. The enzyme degrades laminin, collagen IV, fibronectin and also nidogen. VaH3 is a potent ?-fibrinogenase with weak beta-fibrinogenolytic activity. Its preferes bulky and hydrophobic amino acids at the P1’ position in substrates. It does not activate plasminogen or prothrombin. Partial amino acid sequences demonstrated that VaH3 is a P-III class snake venom metalloproteinase. VaH3 has cytotoxic effects on HeLa tumor cells. It interferes with the adhesion and induces detachment of the cells from Matrigel.

COBISS.SI-ID: 22961703

2.

Crystal structures of two isoforms of the neutrotoxic and anticoagulant PLA2s from Vipera a. ammodytes venom : explanation of functional differences.

Ammodytoxins A and C (AtxA and AtxC) are group IIA sPLA2 isoforms from the venom of Vipera a. ammodytes. They exhibit strong neurotoxic and anticoagulant effects. The two isoforms, which differ in sequence by only two amino acid residues out of 122, display significant differences in toxicity and anticoagulant properties and act on protein targets including activated factor X (FXa) with significantly different strengths of binding. We determined the crystal structures of both isoforms and revealed in this way structural reasons for the observed functional differences between the two toxins.

COBISS.SI-ID: 22513447