Biomedical subjects
Publications and source records attributed to D Mebs.
Thirty-one venom samples from European vipers (genera Vipera and Daboia) were tested for haemorrhagic and myotoxic activity by intramuscular injection into mice. Most venoms exhibited haemorrhagic activity and fewer had myotoxic activity, both of which are not strictly related.
Tetrodotoxin and its analogues, 4-epitetrodotoxin and 4,9-anhydrotetrodotoxin, were detected in the toad Atelopus oxyrhynchus by HPLC analysis. The toxin and its analogues were still present in a specimen which lived 3.5 years in captivity.
After a bite by the aglyphous red-necked keelback snake Rhabdophis subminiatus a complete defibrinogenation syndrome with severe hemorrhagic diathesis developed in a 25-year-old man. In vitro studies showed that the venom gland extract of the snake contains a very active prothrombin (Factor II) activator. The thrombin generated is inhibited neither by antithrombin III nor the antithrombin-III-heparin complex. The venom gland extract stimulated also the tissue plasminogen activator; however, it did not cause direct activation of plasminogen, protein C, Factor X or direct degradation of fibrinogen.
The complete amino acid sequence of a myotoxin isolated from Crotalus adamanteus venom (CAM-toxin) was determined. The total number of amino acid residues was 45, giving a mol. wt of 5202. The amino acid sequence was compared with those of previously determined Crotalus myotoxins. The CAM-toxin shows a surprisingly close relationship to those of peptide c (C. v. helleri), myotoxin a (C. v. viridis), crotamine (C. d. terrificus), myotoxin I and II (C. v. concolor) with homologies of approximately 98, 83, 90, 95 and 91%, respectively. The hydropathy profile of the CAM-toxin is almost identical to peptide c and myotoxin I, as can be assumed from the sequence homology. Despite the absence of any close sequence homology with the myotoxic phospholipase A2 enzymes, CAM-toxin contains a similar cationic myotoxic region at residues 2-10 as found in the other five myotoxic peptides.
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Necrosis of skeletal muscle is produced by two types of snake venom components: single chain peptides consisting of 42-44 amino acid residues and phospholipases A2 representing either single chain proteins or existing as complexes of several enzyme subunits or combined with other nonenzymatic proteins. Vacuolation, lysis and necrosis of skeletal muscle cells are the major pathological effects of these myotoxins. Although the exact mode of action of these toxins is not clear, interactions with the plasma membrane leading to permeability changes for ions and to their complete destruction is evident. The high specificities of some venom phospholipases A2 for skeletal muscle cells suggest a specific binding to certain membrane receptors; however, an enzymatic action on membranes may also be involved.
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Alcohol extracts from the frog Atelopus oxyrhynchus were toxic to mice when injected intraperitoneally. The toxin was purified by gel filtration on a Sephadex G-15 column, and was identified as tetrodotoxin by thin-layer chromatography and GC-MS analysis of the alkali-hydrolyzed and trimethylsilylated derivative giving the same pattern as the C9-base of tetrodotoxin.
Five polyvalent antivenoms (Crotalidae; Orient, North, Central and South Africa) were tested for their ability to neutralize the thrombin-like activity of snake venoms (Bitis gabonica, Agkistrodon acutus, Bothrops asper, B. atrox, Crotalus adamanteus). Considerable cross-neutralization was observed. Anti-coagulase antibodies were isolated from an antivenom by affinity chromatography using a purified enzyme from Bitis gabonica venom. These antibodies neutralized the activity of most snake venom coagulant enzymes.
Neurotoxins isolated from snake venom exhibit very specific actions on nervous structures. Their use in neurobiological research contributed to a better understanding of neuromuscular transmission and led to the isolation of a receptor, the nicotinic acetylcholine receptor.
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One monovalent (habu-antivenom) and five polyvalent antivenoms (Crotalidae; Orient, North, Central and South Africa) were tested for their ability to neutralize the hemorrhagic activity of 12 snake venoms (Agkistrodon, Bothrops, Crotalus, Sistrurus, Trimeresurus, Bitis, Echis spp.) when mixed prior to injection into the hind leg of mice. Considerable cross-neutralization was observed: antivenoms prepared against African snake venoms were equally or more potent in neutralizing the hemorrhagic activity of Crotalidae venoms. The same applies to Crotalidae antivenom which neutralized the activity of African snake venoms. Anti-hemorrhagic antibodies were isolated from a polyvalent antivenom by affinity chromatography using purified hemorrhagins from Bitis arietans and Crotalus adamanteus venom as ligands. These antibodies neutralized the activity of both hemorrhagins indicating common antigenic determinants in these molecules.
While bathing in the Indian Ocean a 31-year-old German woman came into contact with a jelly-fish, probably of the species Chrysaora quinquecirrha. Initial signs were inflammatory cutaneous changes on the upper trunk, and both arms and feet. Over the next few days massive edematous swelling developed over the trunk, in addition to signs of arterial underperfusion in the hands and legs. Under treatment with urokinase and prostaglandin E1 the circulatory disorder in the feet completely disappeared. But the edema on the arms and hands got worse and huge bullae developed. On the assumption of a compartment syndrome a bilateral fasciotomy was performed. Wound healing proceeded normally. However, even after six months there remained extensive sensory and motor defects in both hands and arms.