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PubMed2003

Wide distribution of cysteine-rich secretory proteins in snake venoms: isolation and cloning of novel snake venom cysteine-rich secretory proteins.

Cysteine-rich secretory proteins (CRISPs) are found in epididymis and granules of mammals, and they are thought to function in sperm maturation and in the immune system. Recently, we isolated and obtained clones for novel snake venom proteins that are classified as CRISP family proteins. To elucidate the distribution of snake venom CRISP family proteins, we evaluated a wide range of venoms for immuno-cross-reactivity. Then we isolated, characterized, and cloned genes for three novel CRISP family proteins (piscivorin, ophanin, and catrin) from the venom of eastern cottonmouth (Agkistrodon piscivorus piscivorus), king cobra (Ophiophagus hannah), and western diamondback rattlesnake (Crotalus atrox). Our results show the wide distribution of snake venom CRISP family proteins among Viperidae and Elapidae from different continents, indicating that CRISP family proteins compose a new group of snake venom proteins.

Amino Acid Sequence↗

PubMed1985

Amino acid sequences of phospholipases A2 from the venom of an Australian elapid snake (king brown snake, Pseudechis australis).

Two basic phospholipases A2 (Pa-11 and Pa-13) have been isolated from the venom of an Australian elapid snake, Pseudechis australis (king brown snake). The reduced and S-carboxymethylated phospholipases A2 were digested with trypsin and the resulting peptides were purified by a combination of chromatography on a DEAE-cellulose DE-52 column and gel filtration procedures. Eleven main peptides from Pa-11 and 9 peptides from Pa-13 could account for the amino acid compositions of the respective enzyme molecules. The alignment of the tryptic peptides and unelucidated regions of the amino acid sequences of tryptic peptides were established by the analysis of the peptides obtained by chymotryptic and/or Staphylococcal protease digestions. Each phospholipase A2 consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. Although Pa-11 is enzymatically 30-times as active as Pa-13 and highly toxic as compared to Pa-13, they are highly homologous in their amino acid sequences. They are also homologous to the enzymes from mammalian pancreas and the other snake venom phospholipases A2, especially to those from snakes belonging to the subfamilies Acanthophiinae and Laticaudinae.

Amides↗

PubMed1998

The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases.

BACKGROUND: Trimeresurus stejnejeri venom plasminogen activator (TSV-PA) is a snake venom serine proteinase that specifically activates plasminogen. Snake venom serine proteinases form a subfamily of trypsin-like proteinases that are characterised by a high substrate specificity and resistance to inhibition. Many of these venom enzymes specifically interfere with haemostatic mechanisms and display a long circulating half-life. For these reasons several of them have commercial applications and are potentially attractive pharmacological tools. RESULTS: The crystal structure of TSV-PA has been determined to 2.5 A resolution and refined to an R factor of 17.8 (R free, 24.4). The enzyme, showing the overall polypeptide fold of trypsin-like serine proteinases, displays unique structural elements such as the presence of a phenylalanine at position 193, a C-terminal tail clamped via a disulphide bridge to the 99-loop, and a structurally conserved Asp97 residue. The presence of a cis proline at position 218 is in agreement with evolutionary relationships to glandular kallikrein. CONCLUSIONS: We postulate that Phe 193 accounts for the high substrate specificity of TSV-PA and renders it incapable of forming a stable complex with bovine pancreatic trypsin inhibitor and other extended substrates and inhibitors. Mutational studies previously showed that Asp97 is crucial for the plasminogenolytic activity of TSV-PA, here we identify the conservation of Asp97 in both types of mammalian plasminogen activator - tissue-type (tPA) and urokinase-type (uPA). It seems likely that Asp97 of tPA and uPA will have a similar role in plasminogen recognition. The C-terminal extension of TSV-PA is conserved among snake venom serine proteinases, although its function is unknown. The three-dimensional structure presented here is the first of a snake venom serine proteinase and provides an excellent template for modelling other homologous family members.

Amino Acid Chloromethyl Ketones↗

PubMed2006

Female snake sex pheromone induces membrane responses in vomeronasal sensory neurons of male snakes.

The vomeronasal organ (VNO) is important for activating accessory olfactory pathways that are involved in sexually dimorphic mating behavior. The VNO of male garter snakes is critically important for detection of, and response to, female sex pheromones. In the present study, under voltage-clamp conditions, male snake VNO neurons were stimulated with female sexual attractiveness pheromone. Thirty-nine of 139 neurons exhibited inward current responses (reversal potential: -10.6 +/- 2.8 mV). The amplitude of the inward current was dose dependent, and the relationship could be fitted by the Hill equation. Under current-clamp conditions, application of pheromone produced membrane depolarizing responses and increases in firing frequency. These results suggest that the female pheromone directly affects male snake VNO neurons and results in opening of ion channels, thereby converting the pheromone signal to an electrical signal. The response to female pheromone is sexually dimorphic, that is, the pheromone does not evoke responses in VNO neurons of female snakes. An associated finding of the present study is that the female sex pheromone, which is insoluble in aqueous solutions, became soluble in the presence of Harderian gland homogenate.

Animals↗

PubMed1995

Effects of relaxation training on fear and arousal during in vivo exposure to a caged snake among DSM-III-R simple (snake) phobics.

Eight pairs of DSM-III-R snake phobic subjects (Ss) were exposed to a caged snake while seated in front of a package-conveyor apparatus during eight 4-minute trials. Heart rates and skin-conductance levels were recorded before and during each of the eight trials. Self-reports of fear were obtained after each trial. One S in each pair controlled the conveyor on alternating trials. One subject (S) in each pair had received a representative regimen of relaxation training beforehand. Heart-rate decreased more in Ss controlling the conveyor than in their yoked partners. Ss who had received relaxation training showed lower heart-rate change, lower skin-conductance change, and lower self-reports of fear after the exposure trials. Relaxed Ss also moved the snake closer to themselves than did unrelaxed subjects on some trials.

Adult↗

PubMed1997

Enzymatic properties of the Duvernoy's secretion of Blanding's tree snake (Boiga blandingi) and of the mangrove snake (Boiga dendrophila).

Duvernoy's secretion from representatives of the colubrid genus Boiga has been shown by other workers: (1) to contain an alpha-bungarotoxin-like component (Blanding's tree snake, Boiga blandingi); (2) to exhibit acetylcholine receptor binding activity (the brown tree snake, Boiga irregularis); and (3) to react strongly (B. blandingi and the mangrove snake, Boiga dendrophila) with antisera raised against elapid venoms. The present study provides the first evidence for the presence of acetylcholinesterase, a common elapid enzyme, in the Duvernoy's secretion of B. dendrophila and B. blandingi at levels of 122 +/- 7 and 0.36 +/- 0.02 International Enzyme Units, respectively. Constants for inhibition by eserine were 1.25 x 10(-7) M and 2.79 x 10(-7) M, respectively. The Duvernoy's secretion of B. dendrophila exhibited significant phospholipase and haemolytic activities, whereas phosphodiesterase was only weakly present and no thrombin-like activity was observed.

Acetylcholinesterase↗

PubMed2003

Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibalpha binding mechanism induced by snake venom proteins.

Bitiscetin, a platelet adhesion inducer isolated from venom of the snake Bitis arietans, activates the binding of the von Willebrand factor (VWF) A1 domain to glycoprotein Ib (GPIb) in vitro. This activation requires the formation of a bitiscetin-VWF A1 complex, suggesting an allosteric mechanism of action. Here, we report the crystal structure of bitiscetin-VWF A1 domain complex solved at 2.85 A. In the complex structure, helix alpha5 of VWF A1 domain lies on a concave depression on bitiscetin, and binding sites are located at both ends of the depression. The binding sites correspond well with those proposed previously based on alanine-scanning mutagenesis (Matsui, T., Hamako, J., Matsushita, T., Nakayama, T., Fujimura, Y., and Titani, K. (2002) Biochemistry 41, 7939-7946). Against our expectations, the structure of the VWF A1 domain bound to bitiscetin does not differ significantly from the structure of the free A1 domain. These results are similar to the case of botrocetin, another snake-derived inducer of platelet aggregation, although the binding modes of botrocetin and bitiscetin are different. The modeled structure of the ternary bitiscetin-VWF A1-GPIb complex suggests that an electropositive surface of bitiscetin may interact with a favorably positioned anionic region of GPIb. These results suggest that snake venom proteins induce VWF A1-GPIbalpha binding by interacting with both proteins, and not by causing conformational changes in VWF A1.

Crystallization↗

PubMed1999

Randomized controlled trial on the effective dose of anti-snake venom in cases of snake bite with systemic envenomation.

Snake bite is the common cause of morbidity and mortality in India. Snake antivenom, although very effective, is expensive, scarce, and associated with side effects. The conventional dose may not be required in all cases and a smaller dose may be as effective. A randomized double blind controlled trial was conducted to compare the effect of lower versus the conventional (high) dose. Patients presenting within 24 hours of snake bite with hematological or neurological evidence of systemic envenomation were included in the study. Patients were randomized either to receive high dose (2 vials over 1 hour, followed by 2 vials over 4 hours and repeated 4 hourly until clotting parameters normalized and then 2 vials as infusion over 24 hours) or low dose (2 vials over 1 hour, followed by 1 vial over four hours, repeated 4 hourly until clotting parameters were normalized and then 1 vial as an infusion over 24 hours). Thirty one patients received high dose and 29 a low dose. The mean dose of antivenom used was significantly different in the two groups (8.9 and 4.7, respectively). There was no mortality. The duration of stay was 4.94 and 3.48 days, respectively. There was no difference in the transfusion, dialysis or ventilation requirement of the two groups. Low dose regimen is more effective and required 5 vials less than the conventional dose. Each vial costs Rs. 200, so the estimated savings is Rs. 1000 per patient.

Adult↗

PubMed2004

Rational use of anti-snake venom (ASV): trial of various regimens in hemotoxic snake envenomation.

BACKGROUND: Viperine snake bites cause hemotoxicity in the form of coagulation dysfunction. Optimal dose requirement of anti-snake venom (ASV) and duration of therapy in such situation have not yet been fully explored. Our aim in this study was to compare two low-dose continuous infusion regimes with the standard high dose intermittent bolus regime in treating systemic envenomation and preventing its recurrence. METHODS: A prospective interventional study was conducted on 90 adult patients with snake bite with hemotoxicity. Patents were allocated into three treatment regimes, each regime being tried on 30 patients. Regimen I (standard high dose regimen) consisted of conventional, intermittent bolus dosage of 100 ml of ASV as a loading dose followed by 50 ml every six hours till whole blood coagulation time (CT) became normal. Regimen II consisted of 30 ml of ASV as a loading dose followed by 30 ml continuous infusion every six hours till two CTs at an interval of six hours were normal and a further dose of 30ml over 24 hours. Regimen III was similar to Regimen II in all aspects except that loading dose was 70 ml (instead of 30 ml). RESULTS: In patients with mild envenomation, even though the average requirement of ASV was only marginally lower in Regimen II (128.6 ml) as compared to in Regimen I (137.5 ml), one patient on Regimen I had relapse of coagulation dysfunction. In patients with moderate envenomation, average requirement of ASV was 221.3 ml and 179 ml in Regimens II and III respectively, which was much less than in Regimen I (343.8 ml) (p values 0.05 and 0.01 respectively). Further, no patient receiving Regimen III had relapse of coagulation dysfunction. In severe envenomation, average dose of ASV required was almost similar in Regimens II and III, i.e., 213.7 ml and 233.7 ml respectively, as compared to 433.3 ml required in Regimen I (p values 0.02 and 0.001 respectively). However, time lapse for CT normalization was only 18 hours in Regimen III as compared to 23.6 hours and 24 hours in Regimens I and II respectively. CONCLUSION: Regimens consisting of continuous intravenous infusion of ASV i.e., Regimen II in mild envenomation and Regimen III in moderate and severe envenomation are likely to make significant saving of ASV and reduction of recurrence of coagulation dysfunction.

Adult↗

PubMed1985

Prolonged intensive therapy after snake bite. A probable case of envenomation by the rough-scaled snake.

A case of snake-bite envenomation, probably by the rough-scaled snake (Tropidechis carinatus), in a 9-year-old boy is reported which we believe to represent the most severe and prolonged case yet of non-fatal snake-bite envenomation in a human. The initial clinical features included loss of consciousness within minutes of the bite, followed by a period of partial recovery. The child subsequently developed total body paralysis, acute renal failure, and gross rhabdomyolysis. Artificial ventilation was maintained for 10 weeks; muscle paralysis and paresis persisted for 18 weeks before neuromuscular function returned to normal. Recovery occurred in centripetal fashion, the respiratory muscles and the palatal muscles being the last to recover. Acute renal failure persisted for 18 days and was treated by peritoneal dialysis. Some beneficial effects were seen even when antivenom was given 90 hours after the bite, but gross rhabdomyolysis caused by this species is not prevented by the administration of antivenom after 60 hours. It is concluded that if life can be sustained for 10 weeks by artificial ventilation, normal intellectual and neuromuscular recovery is possible in such cases.

Acute Kidney Injury↗

PubMed1983

Phospholipid hydrolysis in serum lipoproteins by a basic phospholipase A2 from Naja nigricollis snake venom and an acidic phospholipase A2 from Naja naja atra snake venom.

Apparent Km and Vmax values for PC and PE hydrolysis were determined following exposure of HDL, LDL, and VLDL to a basic phospholipase A2 from N. nigricollis snake venom and an acidic phospholipase A2 from N. nigricollis snake venom and an acidic phospholipase A2 from N. n. atra snake venom. Both enzymes hydrolyzed the lipoprotein phospholipids approximately as fast as they hydrolyzed pure phospholipids in mixed micelles, however, the N. nigricollis enzyme, which has a much stronger anticoagulant effect than the N. n. atra enzyme, had lower apparent Vmax values. These values were highest for phospholipids in VLDL and lowest for HDL, however, the differences between the lipoproteins were relatively small with the N. nigricollis enzyme while the differences were much larger with the N. n. atra enzyme. Fractions of the two enzymes in which varying numbers of lysines were carbamylated showed much larger differences in relative rates of phospholipid hydrolysis in HDL, LDL and VLDL. Triton X-100 eliminates these differences in rates of hydrolysis. These results are discussed in terms of the differences in the organized structure of the lipoprotein classes and in the penetration ability of the phospholipases.

Animals↗

PubMed1991

Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis (Australian king brown or mulga snake) venom.

Venoms from 30 different snake species were tested in a disc diffusion assay for antibacterial effects against gram-positive and gram-negative bacteria. A number of venoms gave a zone of inhibition against both groups of bacteria, including Aeromonas hydrophila, an important pathogen of reptiles and amphibians. Two antibacterial components from the venom of an Australian elapid, Pseudechis australis (Australian king brown or mulga snake) were purified to homogeneity. The proteins, designated LAO1 and LAO2, had potent antibacterial properties associated with L-amino acid oxidase activity. Both had native and subunit mol. wts of 142,000 and 56,000, respectively. Antibacterial activity correlated with enzymatic activity and was eliminated with catalase. LAO1 and LAO2 had 244 and 113 units of L-amino acid oxidase activity/mg protein, respectively. Compared to tetracycline, a drug of choice for Aeromonas infections in humans, reptiles and amphibians, the in vitro antibacterial effects of LAO1 and LAO2 were respectively 70 and 17.5 times more effective (on a molar basis).

Aeromonas hydrophila↗

PubMed1994

Inhibition of hemorrhagic activities of various snake venoms by purified antihemorrhagic factor obtained from Japanese Habu snake.

The ability of purified antihemorrhagic factor isolated from the serum of Japanese Habu (Trimeresurus flavoviridis) was tested on 17 snake venoms to inhibit their hemorrhagic activity. The factor strongly inhibited that of the venoms of Crotalus horridus horridus and Vipera latastei gaditana in addition to that of the homologous (T. flavoviridis) venom. Hemorrhagic activity of Agkistrodon halys blomhoffi, Agkistrodon contortrix contortrix, Bothrops atrox asper and Crotalus atrox venoms was also remarkably inhibited, but that of Vipera mauretanica to less extent. The hemorrhagic activities of nine other snake venoms were not inhibited.

Animals↗

PubMed1995

Sphero-echinocytosis of human red blood cells caused by snake, red-back spider, bee and blue-ringed octopus venoms and its inhibition by snake sera.

It was found that bee (Apis mellifera) venom, red-back spider (Latrodectus mactans) venom, blue-ringed octopus (Hapalochlaena maculosa) venom, ten different snake venoms, phospholipase A2 and four snake toxins caused sphero-echinocytosis of human red blood cells at 200 ng/ml. Most venoms and toxins lost the ability to deform human red blood cells when their components of less than mol. wt 10,000 were applied. In a number of cases the sphero-echinocytotic effect was also inhibited by blood sera of Notechis scutatus and Pseudonaja textilis.

Antivenins↗

PubMed1994

Preferential antagonism of the interactions of the integrin alpha IIb beta 3 with immobilized glycoprotein ligands by snake-venom RGD (Arg-Gly-Asp) proteins. Evidence supporting a functional role for the amino acid residues flanking the tripeptide RGD in determining the inhibitory properties of snake-venom RGD proteins.

The inhibitory properties of a panel of snake-venom-derived RGD (Arg-Gly-Asp) proteins, including the disintegrins kistrin, elegantin and albolabrin, and the neurotoxin homologue dendroaspin, were investigated in a platelet-adhesion assay using three immobilized ligands of the glycoprotein IIb-IIIa complex (alpha IIb beta 3), namely fibrinogen, fibronectin and von Willebrand factor (vWF). The snake-venom proteins preferentially inhibited the adhesion of ADP-treated platelets to one or more of the immobilized ligands. Kistrin and dendroaspin exhibited similar inhibitory characteristics, abrogating platelet adhesion to fibrinogen and vWF at nanomolar concentrations, but poorly inhibiting adhesion to fibronectin. Kistrin and dendroaspin share little overall amino-acid-sequence identity, but a considerable level of sequence similarity exists around the RGD tripeptide. Synthetic cyclic peptides corresponding to these regions of kistrin and dendroaspin inhibited platelet adhesion to both fibrinogen and fibronectin with approximately equal potency, but were 100-fold weaker antagonists of the interactions of the alpha IIb beta 3 complex with fibrinogen than their parent proteins. The disintegrins elegantin and albolabrin, which share approx. 60% overall amino-acid-sequence similarity with kistrin but have different residues around the RGD tripeptide, exhibited different antagonistic preferences. Elegantin inhibited platelet adhesion to immobilized vWF and fibronectin, but was significantly less effective at disrupting adhesion to fibrinogen. Albolabrin selectively inhibited platelet adhesion to immobilized vWF and was less effective with fibrinogen and fibronectin as adhesive ligands. In contrast with the behaviour of these venom proteins, the adhesion of ADP-treated platelets to immobilized fibrinogen, fibronectin and vWF was inhibited non-selectively by a range of monoclonal antibodies with specificity for the alpha IIb beta 3 complex. These observations, therefore, define antagonistic preferences in this panel of venom proteins towards the interactions of the alpha IIb beta 3 complex with three immobilized glycoprotein ligands.

Amino Acid Sequence↗

PubMed1981

A snake lady: post-concussion syndrome manifesting visual hallucinations of snakes.

A 37-year-old female was referred to the Department of Psychiatry at the University of Iowa with visual hallucinations of snakes that began ten months after a brief loss of consciousness in a car accident. She also complained about a persistent headache and depressed mood that began shortly after the accident. Her depressive symptoms did not respond to amitriptyline or ECT. By thoroughly reviewing the clinical features and course of this patient, we conclude that the she did not have a typical, definite psychiatric syndrome explaining her hallucinations. The hallucination of snakes in this case may be a manifestation of post-concussional syndrome.

Adult↗

PubMed2005

Snake venomics: comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina.

The protein composition of the crude venoms of the three most important vipers of Tunisia was analyzed by RP-HPLC, N-terminal sequence analysis, MALDI-TOF mass determination, and in-gel tryptic digestion followed by PMF and CID-MS/MS of selected peptide ions in a quadrupole-linear IT instrument. Our results show that the venom proteomes of Cerastes cerastes, Cerastes vipera, and Macrovipera lebetina are composed of proteins belonging to a few protein families. However, each venom showed distinct degree of protein composition complexity. The three venoms shared a number of protein classes though the relative occurrence of these toxins was different in each snake species. On the other hand, the venoms of the Cerastes species and Macrovipera lebetina each contained unique components. The comparative proteomic analysis of Tunisian snake venoms provides a comprehensible catalogue of secreted proteins, which may contribute to a deeper understanding of the biological effects of the venoms, and may also serve as a starting point for studying structure-function correlations of individual toxins.

Amino Acid Sequence↗

PubMed2003

Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: a factor contributing to snake venom variability.

The reprolysin subfamily of metalloproteinases includes snake venom metalloproteinases (SVMP) and mammalian disintegrin/metalloproteinase. These proteins are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP isolated from the venom of Bothrops jararaca. In crude venom, two forms of jararhagin are typically found, full-length jararhagin and jararhagin-C, a proteolytically processed form of jararhagin that is composed of the disintegrin-like and cysteine-rich domains of jararhagin. To better understand the structural and mechanistic bases for these forms of jararhagin in the venom of B. jararaca and the source of venom complexity in general, we have examined the jararhagin forms isolated from venom and the autolysis of isolated jararhagin under the conditions of varying pH, calcium ion concentration, and reducing agents. From our results, jararhagin isolated from venom appears as two forms: a predominant form that is stable to in vitro autolysis and a minor form that is susceptible to autolysis under a variety of conditions including alkaline pH, low calcium ion concentrations, or reducing agent. The autolysis site for production of jararhagin-C from isolated jararhagin was different from that observed for jararhagin-C as isolated from crude venom. Taken together, these data lead us to the conclusion that during the biosynthesis of jararhagin in the venom gland at least three forms are present: one form which is rapidly processed to give rise to jararhagin-C, one form which is resistant to processing in the venom and autolysis in vitro, and one minor form which is susceptible to autolysis under conditions that promote destabilization of its structure. The presence of these different forms of jararhagin contributes to greater structural and functional complexity of the venom and may be a common feature among all snake venoms. The biological and biochemical features in the venom gland responsible for these jararhagin isoforms are currently under investigation.

Amino Acid Sequence↗