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At least 19 recordsLinked to original sources
PubMedDate not supplied

Cross reactivity between venomous, mildly venomous, and non-venomous snake venoms with the Commonwealth Serum Laboratories Venom Detection Kit.

OBJECTIVE: Studies have noted the relatively common occurrence of positive urine results with the Commonwealth Serum Laboratories Venom Detection Kit (VDK) when testing patients with suspected snakebite who are not envenomed. Possible explanations have been false positive test results or subclinical envenoming. We investigated a third possibility, that there is potential for the venom (or saliva) from mildly venomous and non-venomous snakes to give a positive reading with the VDK. METHODS: Venoms/saliva from three non-venomous and seven mildly venomous snake species were tested in the laboratory with the VDK, along with control venoms from four of the five major snake genera (Brown snake, Tiger snake, Death adder and Black snake). RESULTS: Two of the venom/saliva samples, from Gould's hooded snake (Parasuta gouldii), a mildly venomous snake, and the Black-headed python (Aspidites melanocephalus), a non-venomous snake, caused a positive test for the tiger snake genus. There was also cross-reactivity between black snake venoms and the tiger snake well of the VDK. CONCLUSIONS: This study provides a further possible explanation for 'false positive' VDK results, that is venom/saliva presence or absorption from mildly or non-venomous snakes and cross reactivity with venomous snakes on VDK testing. It has implications for antivenom use should it ever be required for more severe envenoming syndromes from mildly or moderately venomous snakes, and for further research. It reinforces the practice of only using VDK testing in patients who show definite evidence of envenoming.

Animals↗
PubMedDate not supplied

Diagnostic uses of snake venom.

Snake venom toxins are invaluable for the assay of coagulation factors and for the study of haemostasis generally. Thrombin-like enzymes (SVTLE) are used for fibrinogen and fibrinogen breakdown product assays as well as detecting dysfibrinogenaemias. Since SVTLE are not inhibited by heparin, they can be used for assaying antithrombin III in samples containing heparin. Snake venom prothrombin activators are utilised in prothrombin assays, whilst Russell's viper venom (RVV) can be used to assay clotting factors V, VII, X and lupus anticoagulants (LA). Activators from the taipan, Australian brown snake and saw-scaled viper have also been used to assay LA. Protein C (PC) and activated PC (APC) resistance can be measured by means of RVV, Protac (from Southern copperhead snake venom) and STA-Staclot (from Crotalus viridis helleri) whilst von Willebrand factor can be studied with Botrocetin (Bothrops jararaca). Finally, snake venom C-type lectins and metalloproteinase disintegrins are being used to study platelet glycoprotein receptors and show great potential for use in the routine coagulation laboratory.

Animals↗
PubMed1984

Enhancement of adenosine 3',5'-monophosphate in human mononuclear and polymorphonuclear leukocytes by snake venoms.

Snake venoms contain compound(s) that enhanced cyclic AMP content in human mononuclear leukocytes maximally after 5 min of incubation at 37 degrees C. The effect was time- and dose-dependent. The half-maximal stimulation of cyclic AMP production by black cobra venom was found at 0.45 micrograms of venom/ml and the value of the Hill coefficient was 0.7. The black cobra venom enhanced the cyclic AMP content in the cells at 4, 22, and 37 degrees C. Similar increase in the cyclic AMP content by six snake venoms was found in human polymorphonuclear leukocytes. The most active venom was from puff adder (Bitis arietans). The data suggest that one of the effects of the snake venoms may be rapid enhancement of cyclic AMP level in the affected cells.

Alprostadil↗
PubMed2003

Subunit dissociation, unfolding, and inactivation of bothrojaracin, a C-type lectin-like protein from snake venom.

Snake venoms contain a large number of hemostatically active proteins that are structurally related to Ca(2+)-dependent animal lectins. These proteins, called C-type lectin-like proteins (CLPs), are generally found as heterodimers composed of two homologous subunits linked by a disulfide bond. Here, bothrojaracin (BJC), a CLP from Bothrops jararaca venom that is also a thrombin inhibitor, has been used as a model to study the subunit dissociation and unfolding of CLPs from snake venom. Dithiothreitol (DTT) up to 10 mM produces minor effects on the tertiary structure and activity of BJC. On the other hand, chromatographic studies and fluorescence polarization measurements indicate that the interchain disulfide bond is disrupted by DTT, although the dimeric association is maintained. Treatment of BJC with urea produces a progressive red shift in the emission spectra of the tryptophan residues, and circular dichroism measurements show that BJC retains significant secondary structure in the presence of 8 M urea, suggesting only partial unfolding. The effects of urea are fully reversible, as there is complete recovery of BJC activity after removal of the denaturing agent. Addition of DTT to a protein sample previously treated with 8 M urea produces a slightly larger spectral shift than that observed with urea alone. Furthermore, in this condition BJC loses its secondary structure, and its subunits are dissociated. After removal of urea and DTT, BJC is inactive toward thrombin, suggesting the irreversibility of their combined action. Altogether, our data show that (i) BJC is highly resistant to urea or DTT effects, requiring the simultaneous action of both agents to fully denature the protein, and (ii) BJC monomers are tightly associated, and the presence of DTT combined with high urea concentrations is necessary to disrupt them. On the basis of these results we propose the first denaturation model for a CLP from snake venom.

Animals↗
PubMedDate not supplied

[Enzymes of snake venoms].

Snakes' venom is a mixture of biologically active substances, containing proteins and peptides. A number of these proteins interact with haemostasis system components. Activators and inhibitors affecting blood coagulation and fibrinolysis systems are of special interest. Venom components can be classified into three main groups, such as procoagulants, anticoagulants and fibrinolytic enzymes according to their action. This review is focused on enzymes from Agkistrodon halys halys venom. They are thrombine-like enzyme, named Ancystron-H, flbrinogenolytic enzyme, protein C activator and platelet aggregation inhibitor. Ancystron-H is used for determination of fibrinogen level in blood plasma of patients undergoing heparin treatment and blood coagulation inhibitors accumulation. The fibrinogenolytic enzyme can be used as the instrument for protein-protein interactions in fibrinogen-fibrin system. The protein C activator is used for protein C level determination in blood plasma with different pathologies. Functions of the platelet aggregation inhibitor, belonging to disintegrins group, can be used for development of antithrombotic preparations. Information about the use of snake venoms in science and medicine is presented.

Ancrod↗
PubMed1995

Antigenic cross-reactivity among components of Brazilian Elapidae snake venoms.

Snake venoms from M. corallinus (LD50 = 7.1 +/- 0.83 micrograms), M. frontalis (LD50 = 19.3 +/- 3.13 micrograms), M. ibiboboca (LD50 = 19.8 +/- 2.07 micrograms) and M. spiixi (LD50 = 6.7 +/- 1.25 micrograms) (family Elapidae, genus Micrurus) injected into horses alone or in combination (M. corallinus with M. frontalis) elicit antibody production, as indicated in vivo by neutralization of venom lethality and in vitro by enzyme-linked immunosorbent assay (ELISA), immunoelectrophoresis (IE) and Western blotting (WB). Venom lethality was efficiently neutralized by the antisera, with the monovalent antivenoms being more efficient than the bivalent antivenom. Antibodies against venom components were detected by all antisera at different titers by ELISA. Upon IE, antisera against M. spiixi and M. frontalis venoms cross-reacted with the four types of venoms studied and recognized several molecular components, the precipitin lines obtained had distinct intensities and electrophoretic motilities, whereas the antivenom against M. corallinus only recognized components of its venom but not of the others. All antivenoms cross-reacted with all the elapid venoms in WB revealing several bands with distinct MWs in M. corallinus and M. spiixi venoms, two very sharp and separate bands in M. corallinus venom and a very sharp band of high MW together with several other smaller and faint bands in M. frontalis venom. The data indicate that snake venoms of the genus Micrurus are good immunogens that contain many cross-reactive molecules, and that their toxic components are neutralized more effectively by monovalent rather than by bivalent antivenom.

Animals↗
PubMed2005

Biological activities of a lectin from Bothrops jararacussu snake venom.

Snake venoms contain saccharide-binding lectins. In this work, we examined the biological activities of a lectin (BjcuL) purified from Bothrops jararacussu snake venom by chromatography on non-derivatized Sepharose 4B and Sephacryl S-200 HR. The protein, a homodimer with subunits of 14.5 kDa, gave a single immunoprecipitin line in immunoelectrophoresis and cross-reacted in ELISA with antivenoms raised against Bothrops spp. (lanceheads), Micrurus spp. (coral snakes), Crotalus durissus terrificus (South American rattlesnake), and arthropod (Loxosceles gaucho, Phoneutria nigriventer and Tityus serrulatus) venoms. BjcuL agglutinated human formaldehyde-fixed erythrocytes at > or = 100 ng/ml and was inhibited by lactose and EDTA (> or = 2 mM) and high concentrations (> 100 mM) of glucose and sucrose, but not by N-acetylglucosamine. BjcuL had no direct hemolytic activity and was devoid of esterase, PLA2 and proteolytic activities. The lectin (up to 200 microg/ml) did not aggregate human platelet-rich plasma (PRP) or washed platelets (WP), nor did it alter the aggregation induced by ADP in PRP or by thrombin in WP. When injected into mouse hind paws, BjcuL (10-100 microg/paw) caused edema and increased vascular permeability, with a maximum effect after 1h that persisted for up to 6 h (edema) or gradually decreased after the peak interval (vascular permeability). No hemorrhage was observed in BjcuL-injected paws. In anesthetized rats, B. jararacussu venom (200 microg/kg, i.v.) produced sustained hypotension (maximum decrease of approximately 60%) whereas a similar dose of BjcuL decreased the blood pressure by approximately 15%, with a rapid return to the resting level.

Animals↗
PubMed1997

Snake venoms.

Snake venoms are complex mixtures containing many different biologically active proteins and peptides. A number of these proteins act on components of the haemostatic system in humans. The paper focuses on those venom constituents that affect the blood coagulation pathway, endothelial cells and platelets. Several highly purified venom enzymes have been used clinically as anticoagulants, and other venom proteins are being used in preclinical research to investigate their possible therapeutic potential. Haemostatically active components are distributed widely in the venom of many different snake species. In no case are all the components described below found in any single venom. Venom components can be grouped into several categories depending on their haemostatic effect. The following haemostatically active components are discussed in this chapter: enzymes that cause fibrinogen coagulation: enzymes that degrade fibrin(ogen); plasminogen activator; prothrombin activators; factor V activator; factor X activator; anticoagulant activities: enzymes with haemorrhagic activity; platelet aggregation inducers: and platelet aggregation inhibitors.

Animals↗
PubMed2006

Molecular characterization and phylogenetic analysis of BjussuMP-I: a RGD-P-III class hemorrhagic metalloprotease from Bothrops jararacussu snake venom.

Snake venom metalloproteases (SVMPs) embody zinc-dependent multidomain enzymes responsible for a relevant pathophysiology in envenomation, including local and systemic hemorrhage. The molecular features responsible for hemorrhagic potency of SVMPs have been associated with their multidomains structures which can target these proteins them to several receptors of different tissues and cellular types. BjussuMP-I, a SVMP isolated from the Bothrops jararacussu venom, has been characterized as a P-III hemorrhagic metalloprotease. The complete cDNA sequence of BjussuMP-I with 1641bp encodes open reading frames of 547 amino acid residues, which conserve the common domains of P-III high molecular weight hemorrhagic metalloproteases: (i) pre-pro-peptide, (ii) metalloprotease, (iii) disintegrin-like and (iv) rich cysteine domain. BjussuMP-I induced lyses in fibrin clots and inhibited collagen- and ADP-induced platelet aggregation. We are reporting, for the first time, the primary structure of an RGD-P-III class snake venom metalloprotease. A phylogenetic analysis of the BjussuMP-I metalloprotease/catalytic domain was performed to get new insights into the molecular evolution of the metalloproteases. A theoretical molecular model of this domain was built through folding recognition (threading) techniques and refined by molecular dynamics simulation. Then, the final BjussuMP-I catalytic domain model was compared to other SVMPs and Reprolysin family proteins in order to identify eventual structural differences, which could help to understand the biochemical activities of these enzymes. The presence of large hydrophobic areas and some conserved surface charge-positive residues were identified as important features of the SVMPs and other metalloproteases.

Amino Acid Sequence↗
PubMed2005

Biochemical and molecular modeling analysis of the ability of two p-aminobenzamidine-based sorbents to selectively purify serine proteases (fibrinogenases) from snake venoms.

Snake venoms contain several trypsin-like enzymes with equivalent physicochemical characteristics and similar inhibition profiles. These are rather difficult to separate by classical purification procedures and therefore constitute a good model for affinity chromatography analysis. Some of these trypsin homologues present fibrinogenase activity, mimicking one or more features of the central mammalian coagulation enzyme, thrombin. It was previously demonstrated that a number of amidine derivatives are able to interact specifically with some of these serine proteases. To understand the enzyme-sorbent interactions we have investigated the ability of two commercially available benzamidine affinity matrices to purify thrombin-like serine proteases (TLSP) with similar biological properties from two snake venoms (Bothrops jararacussu and Lachesis muta rhombeata). Curiously, each sorbent retained a single but distinct TLSP from each venom with high yield. Molecular modeling analysis suggested that hydrophobic interactions within a specific region on the surface of these enzymes could be generated to explain this exquisite specificity. In addition, it was demonstrated that a specific tandem alignment of the two benzamidine sorbents enables the purification of three other enzymes from B. jararacussu venom.

Amino Acid Sequence↗
PubMedDate not supplied

Snake venom proteinases as tools in hemostasis studies: structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom.

Snake venom serine proteinases affect many steps of the blood coagulation cascade. Each of them usually acts selectively on one coagulation factor. They are therefore potentially useful components to study the mechanisms of action, the regulation and the structure-function relationships of human serine proteinase coagulation factors. This strategy is illustrated for a plasminogen activator purified from Trimeresurus stejnegeri venom.

Animals↗
PubMed2005

Serine proteases affecting blood coagulation and fibrinolysis from snake venoms.

Snake venom proteases, in addition to their contribution to the digestion of the prey, affect various physiological functions. They affect platelet aggregation, blood coagulation, fibrinolysis, complement system, blood pressure and nervous system. This review provides a ready reference for serine proteases that interfere in blood coagulation and fibrinolysis. They exhibit their activity by activation of specific zymogens of coagulation factors. These serine proteases serve as tools to study molecular details in the activation of specific factors involved in coagulation and fibrinolytic cascades and are useful in treating various thrombotic and hemostatic conditions.

Animals↗
PubMed1990

Neutralization of hemorrhagic snake venoms by sera of Trimeresurus flavoviridis (Habu), Herpestes edwardsii (mongoose) and Dinodon semicarinatus (Akamata).

The sera of T. flavoviridis (Habu), H. edwardsii (mongoose) and D. semicarinatus (Akamata, non-venomous snake) were tested for their capacity to neutralize 28 species of hemorrhagic snake venoms in vitro. The sera of these animals neutralized a variety of hemorrhagic venoms, suggesting a common structure for a hemorrhagic factor and a similar mechanism of neutralization for the antihemorrhagic factor in the sera. The serum of T. flavoviridis neutralized the lethal toxicity of the T. flavoviridis venom but could not neutralize those of the other hemorrhagic venoms at all. The sera of H. edwardsii and D. semicarinatus did not inhibit the activity of all hemorrhagic venoms.

Animals↗
PubMed2002

Effect of snake venom procoagulants on snake plasma: implications for the coagulation cascade of snakes.

Several snake venoms contain proteinases that activate zymogens in the coagulation cascade and thus exhibit their procoagulant effects. While most procoagulant proteinases from snake venoms are dissimilar to coagulation factors, Group D (trocarin, notecarin) and C (pseutarin) prothrombin activators are structural and functional homologues of factor Xa and the prothrombinase complex, respectively. We examined the effect of these and other procoagulants from snake venoms as well as mammalian and snake thromboplastins on the coagulation of plasmas of Notechis scutatus, Pseudonaja textilis (both procoagulant venoms), Python reticulatus (non-venomous) and Crotalus atrox (non-procoagulant venom) snakes. The results indicate that the intrinsic pathway seems to be weak or absent only in venomous snakes, while the extrinsic pathway is fully functional in all snakes. Python and Crotalus plasmas have extrinsic pathways similar to that in mammals. In contrast, although Notechis and Pseudonaja plasmas were clotted by a Group C activator, they failed to clot upon the addition of factor Xa and Group D activators. The mechanism of this resistance is still elusive.

Animals↗
PubMed2005

Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases.

The importance of proteinases in the pathologies associated with Viperid envenoming has long been appreciated. Over the past 40 years substantial research has clearly implicated metalloproteinases in the venom (snake venom metalloproteinases; SVMPs) as playing key roles in the development of such symptoms as hemorrhage, edema, hypotension, hypovolemia, inflammation and necrosis. In spite of this wealth of information there are still many unresolved questions pertaining to the structural basis for the various SVMPS giving rise to the diversity of activities. In this short review we will not attempt to provide an exhaustive collation of structural studies on the SVMPs; however, we will give a brief outline of the structural classification of the SVMPs; as well as relate them to the other members of the reprolysin family of metalloproteinases, the ADAMs. The information put forth in the text does not allow specific conclusions to be drawn on the structural basis for SVMP functional diversity, but it is our goal that it will allow for the development of testable hypotheses that can be experimentally pursued. What the reader will observe is that there are very interesting structural features displayed by the various SVMP classes and subclasses that provide insight into their functional characteristics.

Amino Acid Sequence↗