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PubMed1989

Enzymatic and toxic properties of Ophiophagus hannah (king cobra) venom and venom fractions.

Some enzymatic activities and toxic properties of four samples of Ophiophagus hannah (king cobra) venom were investigated. There is little intraspecific variation in enzyme contents, protein composition and toxic properties of the venom. The venom does not exhibit hemolytic or edema-inducing activity but is characterized by an exceptionally high alkaline phosphomonoesterase activity. DEAE-Sephacel ion exchange chromatography and Sephadex G-75 gel filtration chromatography of the venom indicate that the major lethal toxins are the low mol.wt, non-enzymatic basic proteins. Venom fractions exhibiting high enzymatic activities apparently do not play an important role in the lethality in mice of Ophiophagus hannah venom.

Animals↗
PubMed1989

Hemolytic activity of thionin from Pyrularia pubera nuts and snake venom toxins of Naja naja species: Pyrularia thionin and snake venom cardiotoxin compete for the same membrane site.

Pyrularia thionin (P. thionin) is a strongly basic peptide of 47 amino acids which is hemolytic, cytotoxic and neurotoxic. It shows the greatest hemolytic activity toward human erythrocytes. Rabbit, guinea pig and pig erythrocytes show decreasing activity in that order, and little or no activity is shown with sheep, horse, cow or mouse erythrocytes. Crotalus venoms are inactive, but the venoms from Naja naja atra, Naja naja ceylonicus and Naja naja melanoleuca and, more specifically, cardiotoxin from Naja naja kaouthia have significant hemolytic activities toward human erythrocytes. The cardiotoxin preparation used had no phospholipase activity, and was less active than P. thionin (23% compared to 35% hemolysis by P. thionin in 60 min at 10 micrograms/ml toxin). Since iodinated P. thionin is inactive, it was used as an inhibitor of hemolysis catalyzed by native P. thionin, N. ceylonicus venom and by cardiotoxin. Examination of the kinetics of the reactions catalyzed by N. ceylonicus venom and cardiotoxin in the absence and presence of iodinated P. thionin shows that both N. ceylonicus venom and cardiotoxin exhibit Michaelis-Menten kinetics, yielding apparent Km values of 7.4 micrograms/ml and 0.69 microM, respectively. These values compare to an apparent Km for P. thionin of 1.6 microM for erythrocyte hemolysis and a binding constant of 2.1 microM (Osorio e Castro, V. R. Van Kuiken, B. A. and Vernon, L. P. (1989) Action of a thionin isolated from nuts of Pyrularia pubera on human erythrocytes. Toxicon 27, 501). The inhibition constants Ki for iodinated P. thionin in the reactions with N. ceylonicus venom and cardiotoxin are 3.8 and 5.3 microM, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

Antimicrobial Cationic Peptides↗
PubMed1991

Neutralization of myotoxic activity of Bothrops venoms by antisera to purified myotoxins and to crude venoms.

A phospholipase myotoxin (MOO-1) and a non-phospholipase myotoxin (JSU-5) were studied for their antigenic cross-reactivity and neutralization by different antisera. Antisera against JSU-5 and MOO-1 reacted equally with both myotoxins in ELISA assays. The specificity of these antisera was also similar, recognizing the same 14,000-18,000 mol. wt components in the venoms of Bothrops jararacussu, Bothrops moojeni, Bothrops neuwiedi and Bothrops pradoi. Using creatine kinase assays, JSU-5 myotoxicity was completely neutralized by B. jararacussu antivenom or anti-JSU-5 antibodies and partially neutralized by B. moojeni antivenom or anti-MOO-1 antibodies. MOO-1 myotoxicity was completely neutralized by antisera against JSU-5 and MOO-1 and B. jararacussu antivenom, and only partially neutralized by B. moojeni antivenom. B. jararacussu venom induced high titres of antibodies against purified myotoxins. This antiserum completely inhibited the myotoxicity of the homologous venom and significantly reduced the myotoxicity of the remaining myotoxin-containing venoms. It is suggested that B. jararacussu venom is a good immunogen to induce antibodies against myotoxins present in the venoms of the different species of Bothrops.

Animals↗
PubMed1993

Venom of an aggressive African Theraphosidae (Scodra griseipes): milking the venom, a study of its toxicity and its characterization.

Two milking procedures, electric stimulation and lure-biting, are described and compared. The amount of crude Scodra griseipes venom collected in 3 years by lure-biting was 1670 mg and 1380 mg, respectively, for young females and adult males. The crude venom appears pure on the basis of UV-Vis spectra, which show no hemocyanin absorption bands. The toxicity and induced symptoms of these venoms in mice were evaluated by direct bites and also by LD50 [LD50 (young female venom, i.v.) = 8.1 mg/kg, LD50 (adult male venom, i.v.) > 9.5 mg/kg]. The venom from both sexes was compared by protein content, UV-Vis and 1H-NMR spectroscopies, polyacrylamide gel electrophoresis [SDS-PAGE] and size exclusion high performance liquid chromatography [SE-HPLC]. Differences were observed.

Animals↗
PubMed1993

The effect of the viper Cerastes cerastes cerastes venom and venom fractions on carbohydrate metabolism.

The effect of the viper Cerastes cerastes cerastes venom and venom fractions on carbohydrate metabolism. Toxicon 31, 791-801, 1993.--I.p. injection of a sublethal dose of Cerastes cerastes cerastes venom into white rats induced a marked hypoglycemia after 15 min. This hypoglycemia continued for at least 24 hr. Hypoglycemia was accompanied by a significant increase of liver and muscle glycogen at 15-30 min and 8 hr. Plasma lactate levels were significantly increased for most of the 24 hr test period, and was accompanied by a marked decrease of liver lactate levels. Levels of skeletal muscle lactate increased significantly. Viper venom significantly increased levels of plasma, liver and skeletal muscle pyruvate for most of the 24 hr test period. Cerastes cerastes cerastes venom was fractionated using gel filtration into six fractions. Each of the first four fractions caused a significant hypoglycemic effect at some point of the 6 hr test period, while fraction I also produced a hyperglycemia 30 min after administration. Fraction III, the only fraction to show a continuous hypoglycemic effect during the 6 hr test period, significantly increased plasma insulin levels 30 min after treatment. It is suggested that the hypoglycemia may be due to a direct effect of venom components on plasma insulin levels.

Animals↗
PubMed1982

Modulation of venom-induced leukocyte histamine release by mononuclear cells: effect of venom immunotherapy.

Leukocyte histamine release and blood mononuclear cell proliferative responses to venoms were evaluated in nine patients with sting anaphylaxis. The effect of venom-activated mononuclear cells on the autologous mononuclear cell proliferative response and venom-induced leukocyte histamine release was also studied before and on maintenance immunotherapy. The mononuclear cell proliferative response was low (specific incorporations less than 2.0) and antigen nonspecific both before and during maintenance immunotherapy. Venom-induced in vitro leukocyte histamine release did not change significantly with immunotherapy. However, when patients were on maintenance immunotherapy, venom-activated mononuclear cells cocultured with autologous leukocytes significantly (p less than 0.05) suppressed venom-induced histamine release. The suppressive effect of mononuclear cells was antigen specific and enhanced by in vitro mononuclear cell activation. Suppression of leukocyte histamine release by mononuclear cells extends the regulatory potential of these cells and may identify an additional mechanism by which immunotherapy protects Hymenoptera-sensitive individuals against systemic anaphylaxis.

Adult↗
PubMed1983

Antibodies to purified bee venom proteins and peptides. I. Development of a highly specific RAST for bee venom antigens and its application to bee sting allergy.

IgE antibodies to purified proteins and peptides from honeybee venom have been measured by the RAST. Trace amounts (less than 0.1%) of the major venom protein phospholipase A2 (PLA2) grossly distorted the measurement of IgE antibody to the other venom proteins, acid phosphatase (Acid P) and hyaluronidase (HYAL), and overemphasized their importance. Reduction of antigen coupled to the cellulose paper discs, which were used in the assay, diluted out the contaminating PLA2 without apparent loss in sensitivity. The reduction of disc-bound antigen increased the competition between IgE and IgG antibodies but did not affect measurement of IgE antibodies in sera taken from 35 untreated patients who had a history of general allergic reactions to bee stings. In 54% of sera from bee venom--allergic patients, the greatest IgE antibody response was to PLA2. In all, IgE antibodies to PLA2 were present in 91% of these sera. IgE antibodies to Acid P, HYAL, or melittin were present in 60%, 51%, and 31% of sera, respectively, and accounted for the highest level of binding in 17%, 17%, and 6% of these. Only 6% of sera were positive for whole venom but negative for the isolated antigens. A low level of IgE antibody was found to peptide 401 in 6% of sera. No IgE antibodies were found to apamin. While confirming the central role played by PLA2 in bee sting allergy, these results show that other venom components are also important in some patients.

Acid Phosphatase↗
PubMed1990

Allergens in Hymenoptera venom. XXII. Comparison of venoms from two species of imported fire ants, Solenopsis invicta and richteri.

Venoms were collected by electrical stimulation from the two major species of imported fire ants found in the United States, Solenopsis invicta (Sol i) and S. richteri (Sol r). Antigens similar to three of the four known Sol i venom proteins (I, II, III, and IV) were isolated from Sol r. The N-terminal amino acid sequences for the antigens III were identical; but those for the antigens II demonstrated only nine of 20 residues to be identical. Two monoclonal antibodies raised against Sol i II did not react to Sol r. No protein IV could be detected in Sol r by molecular weight, charge, or immunologically with either polyclonal mouse antibodies or five monoclonal antibodies. Both venoms were compared with a panel of 60 sera from Sol i-allergic individuals; mean bindings were similar with an r = 0.94 for linear regression. RAST inhibition was performed with 17 individual sera representing a variety of Sol i allergen specificities. Four sera were tested from patients resident in the Sol r endemic area and five sera from patients who experienced reactions to S. xyloni stings. All sera reacted comparably to both imported fire ant venoms. The two venoms appear to be allergenically similar, although antigen IV is absent from Sol r and the antigens II have significant sequence variation. Sol i venom appears to be sufficient for diagnostic purposes.

Allergens↗
PubMed1991

In-hospital sting challenge in insect venom-allergic patients after stopping venom immunotherapy.

Immunotherapy (IT) in venom-allergic patients has been demonstrated to provide a highly efficient protection from severe reactions to a re-sting. It is not known whether this protection will persist after IT is stopped in patients with remaining venom sensitivity. In 25 adult patients with a previous severe systemic reaction to a Hymenoptera insect sting, 28 in-hospital sting challenges after stopping IT resulted in no systemic reactions. The mean duration of venom IT was 42.8 months (range, 36 to 83 months), and the mean time interval from the time IT was stopped until sting challenge was, in mean, 25.2 months (range, 12 to 36 months). The mean venom-specific IgE after stopping IT was 2.4 PRU/ml (range, 0 to 16.9 PRU/ml), at the day of sting challenge, 2.7 PRU/ml (range, 0 to 22 PRU/ml), and 2 weeks later, 2.4 PRU/ml (range, 0.02 to 27.8 PRU/ml). These changes in IgE were not significant. Venom-specific IgG concentration when IT was stopped was 64 PU/ml (range, 20 to 144 PU/ml), decreasing significantly to the day of sting challenge to 41.1 PU/ml (range, 13 to 84 PU/ml), and 2 weeks later, a significant increase to a mean of 53.5 PU/ml (range, 12 to 117 PU/ml) was found. Our results suggest that venom IT may be stopped after 3 years, regardless of the level of specific antibodies. To confirm this finding, a larger number of patients should be studied.

Adult↗
PubMed2005

Specific distribution of VEGF-F in Viperinae snake venoms: isolation and characterization of a VGEF-F from the venom of Daboia russelli siamensis.

Vascular endothelial growth factor exerts multiple functions through binding to two distinct receptor tyrosine kinases, Flt-1 and KDR. We previously demonstrated that snake venom VEGFs, designated VEGF-Fs, exhibit potent biological activities when compared with VEGF165 and that they selectively recognize KDR. We herein report the screening of several snake venoms for VEGF-Fs using antibodies against vammin and HF, VEGF-Fs derived from the venom of Vipera ammodytes ammodytes and Vipera aspis aspis, respectively. Specific immunoreactivity was observed in the venoms of Vipera and Daboia species. The present results suggest that VEGF-Fs are specific components of venoms from the Viperinae snakes that inhabit Europe, India, and Asia. We also report the isolation and characterization of an additional VEGF-F from Daboia russelli siamensis venom.

Amino Acid Sequence↗
PubMed2006

Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals novel alpha9beta1 integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases.

Echis ocellatus is the most medically important snake in West Africa. However, the composition of its venom and the differential contribution of these venom components to the severe haemorrhagic and coagulopathic pathology of envenoming are poorly understood. To address this situation we assembled a toxin transcriptome based upon 1000 expressed sequence tags (EST) from a cDNA library constructed from pooled venom glands of 10 individual E. ocellatus. We used a variety of bioinformatic tools to construct a fully annotated venom-toxin transcriptome that was interrogated with a combination of BLAST annotation, gene ontology cataloguing and disintegrin-motif searching. The results of these analyses revealed an unusually abundant and diverse expression of snake venom metalloproteinases (SVMP) and a broad toxin-expression profile including several distinct isoforms of bradykinin-potentiating peptides, phospholipase A(2), C-type lectins, serine proteinases and l-amino oxidases. Most significantly, we identified for the first time a conserved alpha(9)beta(1) integrin-binding motif in several SVMPs, and a new group of putative venom toxins, renin-like aspartic proteases.

Amino Acid Motifs↗
PubMed2005

Functional structure of Agelena labyrinthica's (Araneae:Agelenidae) venom gland and electrophoresis of venom.

The funnel-web spider, Agelena labyrinthica, is widely distributed throughout Turkey. The objective of the present study was to describe the histological and functional fine structure of A. labyrinthica's venom gland by using light microscope, scanning (SEM) and transmission electron microscope (TEM). We have also preliminarily analyzed venom components by SDS-PAGE. Each venom gland has surrounded by a thin adventitia and gross striated muscular bundles. Basal lamina underlies between muscular bundles and the inner glandular epithelium, and ties up them each other. The striated muscular bundles spirally covered venom gland has been observed by SEM. Intricate relations formed between motor neuron axons and the muscle fibers have been revealed by TEM. The secretory epithelium, which made up of simple columnar cells, formed the secretory region of the venom gland. The secretory surface of the gland was increased by a sort of fringes extended from basal membrane into the gland lumen. The epithelial cells have many rough endoplasmic reticulum, mitochondria and different size and shape of secretory granules. These granules have been accumulated in apical portion of the secretory cells. After the gland is emptied, the apical portions of secretory cells deteriorate and the basal epithelial cells regenerate the columnar cells. The analysis of A. labyrinthica venom, which was achieved by SDS-PAGE showed that there have been at least seven components ranging from 10 to 40 kDa molecular weight.

Animals↗
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↗
PubMed1998

Envenomation of mice by Thai cobra (Naja kaouthia) venom: tolerable venom concentration and exposure time.

Naja kaouthia venom appeared in circulation rapidly after intramuscular injection into mice. The venom concentration attained a maximum level with all doses examined after 20 min. The half value of the maximum level was obtained 1 min after injection when a dose of 4LD50 was used. A critical venom concentration endangering mice was assessed from venom concentration in the sera of mice envenomed with sublethal dose (LD50). A fatal condition was produced within 30 min at a venom concentration of 200-300 ng/ml or within 50 min at a venom concentration of 100-150 ng/ml.

Animals↗
PubMed2004

Suction for venomous snakebite: a study of "mock venom" extraction in a human model.

STUDY OBJECTIVE: We determine the percentage of mock venom recovered by a suction device (Sawyer Extractor pump) in a simulated snakebite in human volunteers. METHODS: A mock venom (1 mL normal saline solution, 5.0 mg albumin, 2.5 mg aggregated albumin) radioactively labeled with 1 mCi of technetium was injected with a curved 16-gauge hypodermic needle 1 cm into the right lateral lower leg of 8 supine male volunteers aged 28 to 51 years. The Sawyer Extractor pump was applied after a 3-minute delay, and the blood removed by suction was collected after an additional 15 minutes. A 1991 Siemens Diacam was used to take measurements of the radioactive counts extracted and those remaining in the leg and body. RESULTS: The "envenomation load," as measured by mean radioactivity in the leg after injection, was 89,895 counts/min. The mean radioactivity found in the blood extracted in the 15 minutes of suction was 38.5 counts/min (95% confidence interval [CI] -33 to 110 counts/min), representing 0.04% of the envenomation load. The postextraction leg count was less than the envenomation load by 1,832 counts/min (95% CI -3,863 to 200 counts/min), representing a 2.0% decrease in the total body venom load. CONCLUSION: The Sawyer Extractor pump removed bloody fluid from our simulated snakebite wounds but removed virtually no mock venom, which suggests that suction is unlikely to be an effective treatment for reducing the total body venom burden after a venomous snakebite.

Adult↗
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↗
PubMed2003

One scorpion, two venoms: prevenom of Parabuthus transvaalicus acts as an alternative type of venom with distinct mechanism of action.

Scorpion venom is a complex mixture of salts, small molecules, peptides, and proteins. Scorpions employ this valuable tool in several sophisticated ways for subduing prey, deterring predators, and possibly during mating. Here, a subtle but clever strategy of venom utilization by scorpions is reported. Scorpions secrete a small quantity of transparent venom when initially stimulated that we propose to name prevenom. If secretion continues, a cloudy and dense venom that is white in color is subsequently released. The prevenom contains a combination of high K(+) salt and several peptides including some that block rectifying K(+) channels and elicit significant pain and toxicity because of a massive local depolarization. The presence of high extracellular K(+) in the prevenom can depolarize cells and also decrease the local electrochemical gradient making it more difficult to reestablish the resting potential. When this positive change to the K(+) equilibrium potential is combined with the blockage of rectifying K(+) channels, this further delays the recovery of the resting potential, causing a prolonged effect. We propose that the prevenom of scorpions is used as a highly efficacious predator deterrent and for immobilizing small prey while conserving metabolically expensive venom until a certain level of stimuli is reached, after which the venom is secreted.

Animals↗
PubMed2002

Studies on toad venom (3): effect of metals on the quality of toad venom torrefied on a metal plate.

To study the quality of toad venom dried on different metal plates by heating at 105 degrees C, each 20 g sample of fresh toad venom collected in Hei-Long-Jiang Province, China, was dried on (1) brass, (2) copper, (3) glass, (4) acrylic resins, (5) aluminum and (6) stainless-steel, respectively. Twelve bufadienolides, including bufalin and bufotalin, in each sample were then quantitatively analyzed by HPLC. The total levels of bufadienolides in 1000.0 mg of the dried samples were (1) > (2) > (3) > (4) > (5) > (6), varying from 303.44 mg to 420.72 mg. Besides, the color of dried venom became darker in the order of (2), (4), (6), (3), (1) and (5). Though (1) was not in good color, it was superior to the others in chemical quality. These results suggest that it is possible to dry toad venom in short period by heating it at a high temperature on a tray made of brass. This will be a better method for making high quality toad venom than the traditional method. Moreover, the removal of impurities in the fresh venom by the process of filtration through silk succeeded in raising the bufadienolides content significantly.

Amphibian Venoms↗