Vipera aspis

Audebert F, Urtizberea M, Sabouraud A et al. (1994) Pharmacokinetics of Vipera aspis vemom after experimental envenomation in rabbits. J Pharmacol Exp Ther 268(3) 1512—1517... 

Common Name(s) Cleopatra s Asp, Sahara Sand Viper Vipera Aspis... 

Reperant J. Rio JP, Ward R, Wasowicz M, Miceli D, Medina M, Pierre J (1997) Enrichment of glutamate-like immunoreactivity in the retinotectal terminals of the viper Vipera aspis an electron microscope quantitative immunogold study. J Chem Neuroanat 72 267-280. 

Naulleau, G., 1966, La Biologie et le Comportement Prddateur de Vipera aspis au Laboratoire et dans la Nature, These. P. Fanlac, Paris as reported by Burghardt, 1970a. 

Baumann, F., 1929, Experimente Uber den Geruchssinn und den Beuteerwerb der Viper (Vipera aspis L.), Z. Vergl. Physiol., 10 61. 

Baumann, F. 1929. Experimente iiber den Geruchsinn und den Beuteerwerb der Viper Vipera aspis). Z. vergl. Physiol. 10 36-119. 

The ophio-Z-amino acid oxidase was discovered in the venom of Vipera aspis, V. libetina, V. latastei, BorUirops atrox, Naja sp., etc. and was studied by Zeller and Maritz (146,147). It is differentiated from Z>amino acid oxidase of tissues of higher animals by its inability to oxidize Z-pro-line, Z-oxyproline, and ZV-methyl-Z-leucine and its insensitivity toward ammonium sulfate (148). Otherwise, it produces the same oxidative deamination reactions and acts particularly on Z-methionine. 

The third type of myonecrotic toxins is the type of toxins that possesses both hemorrhagic and myonecrotic actions. Examples are viriditoxin (Fabiano and Tu, 1981), HTb from Crotalus atrox (Ownby et al., 1978), and a hemorrhagic factor from Vipera aspis aspis (Komori and Sugihara, 1988). 

Komori, Y, and Sugihara, H. (1988). Biological study of muscle degenerating hemorrhagic factor from the venom of Vipera aspis aspis (aspic viper). Int. J. Biochem. 20 1417-1423. 

A prospective enquiry was conducted in 1990 and 1991 in France by the Unite des Venins in order to collect epidemiological, clinical and biological data from hospitals. Vipera aspis venom antigens were quantified in urine and blood samples by a sandwich enzyme linked immunosorbant assay. 

Figure 1. Pharmacokinetics of Vipera aspis venom after intravenous (A) and intramuscular (B) administration. Rabbits were injected with Vipera aspis venom via an intravenous route with 250 iLig.kg (A) or via an intramuscular route with 700 iig.kg (B). Plasma samples were collected at the indicated times and assayed by ELISA. Venom concentrations are expressed in nanograms per milliliter as mean s.e.m (n = 5).

Table 3. Kinetic parameters for Vipera aspis venom after intravenous and intramuscular injections...

Figure 2. Effect of antivenom administration on plasma disposition of Vipera aspis venom in experimentally envenomed rabbits. Five rabbits were intramuscularly injected with 700 pg.kg of I-labelled Vipera aspis venom. Seven hours later, they were intravenously injected with 2.5 ml of Ipser Europe serum diluted with 2.5 ml of saline. Plasma samples were analyzed by ELISA for their content in free antigens (O) and by counting radioactivity for their total concentration of antigens ( ).

The effect of antivenom administration on the kinetics of Vipera aspis envenomation was also examined. Radiolabelled Vipera aspis venom was injected intramuscularly to mimic the route of administration in case of accidental envenomations. The use of a radiolabelled venom allowed the quantification of plasma venom components free and bound to antivenom antibodies. Free venom proteins were detected by ELISA. The plasma concentration time profile of venom in antivenom-treated animals is shown in Figure 2. The plasma concentration curves measured by counting radioactivity or by ELISA superimposed before the administration of the antivenom. After intravenous injection of 125 mg of IPSER Europe serum, the total venom concentrations in plasma rapidly increased more than ten-fold and remained elevated during three days, whereas the plasma levels of free venom antigens measured by ELISA rapidly decreased and remained undetectable for the same period of time. Antivenom Fab 2 administration therefore results in the immunocomplexation of venom proteins in the vascular compartment and in the plasma redistribution of venom antigens from the extravascular compartment to the vascular compartment. 

Audebert, F., Urtizberea, M., Sabouraud, A., Scherrmann, J.-M. and Bon, C. (1994b) Pharmacokinetics of Vipera aspis venom after experimental envenomation in rabbits. J. Pharmacol Exp. Then 268, 1512. 

---