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At least 19 recordsLinked to original sources
PubMedDate not supplied

[The efficacy of the bothropic-crotalic antivenom in the neutralization of the main Bothrops jararacussu venom effects].

Myonecrosis is one of the effects of Bothrops jararacussu venom, from which a myotoxin was isolated showing structural homology to phospholipase A2 (PLA2), but without enzymatic activity. Such myotoxic activity is also present in the Crotalus durissus terrifucus venom, and is attributed to crotoxin and to PLA2 (crotoxin B), the basic component of the crotoxin complex. The Bothrops jararacussu venom showed three proteins with immunologic identity to PLA2 from crotoxin. The bothropic (AB) and the bothropic/crotalic (AB/C) anti-venoms, two commercial polyvalent anti-venoms produced at Instituto Butantan, were compared in order to assess their capacity for neutralization of the lethal, hemorrhagic, coagulant and myotoxic activities of Bothrops jararacussu venom. Both anti-venoms showed the same level of hemorrhagic activity neutralization. However, AB/C was about three times more efficient than AB in neutralizing the myotoxic activity, and two times more potent for neutralization of lethality and coagulant activity of Bothrops jararacussu venom. These data suggest that the use of AB/C could be of value in the treatment of patients bitten by snakes of this species.

Animals↗
PubMedDate not supplied

Análisis clínico y epidemiológico de los accidentes por mordeduras de serpientes del género Bothrops en Venezuela [A clinical and epidemiological analysis of accidental bites by snakes of the genus Bothrops in Venezuela].

Clinical register of 60 patients bitten by Bothrops snake who assisted at Leopoldo Manrique Hospital and the Institute of Tropical Medicine (HLM-IMT) in Caracas during 1996-1997 were analysed. The accident was more frequent in males (45/75%). In 32 cases (53.3%) the snake was classified and 26 were Bothrops lanceolatus, 4 Bothrops venezuelensis and 2 Bothrops atrox. Anatomic regions more frequent bitten were superior members (40/66.6%): hands (36/60%), forearm (2/3.3%), elbow (1/1.6%) and arm (1/1.6%). On inferior members (20/33.3%): legs (6/10%), feet (10/16.7%), ankle (2/3.3%), and the hip (2:3.3%). The most frequent clinical manifestations in moderate and severe cases (33 patient) were pain (100%), oedema (98%), ecchymosis (76%), blisters (20%), necrosis (12%), abscess (6%) bleeding (19%), heart failure (1/1.6%), renal failure (1/1.6%). The blood clotting was evaluated in 60 (100%) cases and it was altered in 33 (55%) patients. No deaths were recorded.

Adolescent↗
PubMed2000

Efficacy of bothropic antivenom and its IgG(T) fraction in restoring fibrinogen levels of Bothrops jararaca envenomed mice.

Bothropic antivenom and its IgG(T) fraction, administered 4 h after experimental envenoming by Bothrops jararaca in Swiss mice, were compared for their abilities to restore fibrinogen 24 or 48 h after treatment. IgG(T) was able to normalise fibrinogen levels as efficiently as conventional antivenom. As IgG(T) also neutralises most anti-toxic activities of Bothrops venom, our results suggest that IgG(T) could be a better alternative treatment for envenoming due to the reduced amount of extraneous proteins, which may facilitate the induction of early adverse reactions.

Animals↗
PubMed1992

Neutralization of different activities of venoms from nine species of Bothrops snakes by Bothrops jararaca antivenom.

Antivenoms are the usual treatment in cases of systemic envenoming by Bothrops snakes. However, the neutralization of each venom component by the antivenom is not well established. Bothrops jararaca antivenom, produced in rabbits, recognizes the venoms of nine different Bothrops species with high ELISA antibody titres. Western blot analysis showed that almost all antigens present on both homologous and heterologous venoms are recognized. Neutralization tests were performed using whole antivenom or its IgG fraction. The antivenom was able to neutralize the haemorrhagic, coagulant and necrotizing activities of the heterologous venoms in the same antivenom/venom proportion as for the homologous venom. Myotoxic activity was only partially neutralized. Neutralization of the proteolytic activity of heterologous venoms required higher amounts of antivenom than for the homologous venom. Phospholipase and oedema-inducing activities were completely neutralized only in the homologous system.

Animals↗
PubMed1993

Lipoxygenase-derived mediators may be involved in in vivo neutrophil migration induced by Bothrops erythromelas and Bothrops alternatus venoms.

Bothrops erythromelas (BEV) and B. alternatus (BAV) venoms induced a dose-dependent neutrophil migration when injected into rat peritoneal cavities (20-160 micrograms/cavity). These venoms (80 micrograms/rat) also induced neutrophil migration in the air pouch model of inflammation. This migratory response seemed to be related to the phospholipase A2 (PLA2) activity of the venoms. BAV had approximately two times more PLA2 activity than BEV, and the neutrophil migration induced by the former venom was two to three-fold greater than that observed with the latter. Heated (90 degrees C for 5 min) BEV lost about 50% of its PLA2 activity and this was accompanied by a corresponding loss in the ability to induce neutrophil chemotaxis. Dexamethasone (0.5 mg/kg, s.c.), an indirect inhibitor of PLA2 activity, also abolished the neutrophil migration induced by both venoms. Since NDGA (100 mg/kg, s.c.) and dexamethasone, but not indomethacin (2 mg/kg, s.c.), strongly reduced the neutrophil migration induced by both bothropic venoms, it is suggested that arachidonate-derived lipoxygenase metabolites such as leukotriene B4 act as the chemotactic mediators. Macrophages could be the main cellular source of such metabolites since they are the predominant resident cells in the rat air pouch, and the migratory response of BEV and BAV into peritoneal cavities was potentiated in rats pretreated with thioglycollate. The neutrophil migration induced by BEV and BAV was not due to endotoxin contamination since heated BEV showed no effect and polymyxin B-treated BAV still remained active.

Animals↗
PubMed1997

Chemical modification of histidine and lysine residues of myotoxic phospholipases A2 isolated from Bothrops asper and Bothrops godmani snake venoms: effects on enzymatic and pharmacological properties.

Lysine and histidine residues of two myotoxic phospholipases A2, Bothrops asper myotoxin III and Bothrops godmani myotoxin I, were chemically modified in order to study the effects of these treatments on enzymatic and pharmacological properties. After lysine acetylation the overall basicity of these toxins was lost and their enzymatic activity was significantly reduced, although a residual effect remained, which corresponded to 25% of the activity of native toxins. This treatment abolished both myotoxic and anticoagulant effects, and partially reduced liposome-disrupting activity. Histidine alkylation with p-bromophenacyl bromide affected phospholipase A2, myotoxic and anticoagulant effects in a parallel way. After 24 hr of incubation with the alkylating reagent, these three activities were totally inhibited, in contrast to the liposome-disrupting effect which was only partially affected by this treatment. It is suggested that; (1) catalytic activity plays a role in the pharmacological effects of these myotoxins; (2) lysine residues are relevant for the toxic effects induced by these phospholipases A2; and (3) despite the apparent relevance of enzymatic activity to the pharmacological properties of these toxins, the dissociation observed in lysine acetylation experiments suggests that these myotoxins have a molecular region, different from the catalytic site, which might be also involved in the toxic effects observed.

Acetophenones↗
PubMed2000

Increments in serum cytokine and nitric oxide levels in mice injected with Bothrops asper and Bothrops jararaca snake venoms.

Changes in serum levels of several cytokines and nitric oxide were studied in BALB/c mice injected intraperitoneally with one median lethal dose (LD(50)) of the venoms of Bothrops asper and Bothrops jararaca, two of the medically most important poisonous snakes of Latin America. Despite differences observed in the time-course of cytokine increments and in serum cytokine levels, both venoms induced prominent elevations of TNF-alpha, IL-1, IL-6, IL-10 and IFN-gamma. There was an early increase in TNF-alpha and IL-1, followed by a more pronounced increment by 18 h. IL-6 levels peaked between 4 and 6 h, and this cytokine probably modulates the secretion of TNF-alpha and IL-1 and the synthesis of acute-phase proteins. Both venoms induced an early increment in serum IL-10, whereas IFN-gamma levels reached higher values in mice injected with B. jararaca venom than in those receiving B. asper venom. Serum nitric oxide concentration increased in mice injected with both venoms rapidly after envenomation, remaining elevated for 24 h. It is concluded that a complex pattern of cytokine and nitric oxide synthesis and secretion occurs in severe experimental envenomation by B. asper and B. jararaca venoms. Furthermore, it is suggested that some of these mediators, particularly TNF-alpha, IL-1 and nitric oxide, might play a relevant role in the pathophysiology of systemic alterations induced by these venoms.

Animals↗
PubMedDate not supplied

[Effect of reduction in the Bothrops antivenin dose administrated in patients bitten by the Bothrops snake].

Seven hundred and thirty accidents by Bothrops snake bite attended at Hospital Vital Brazil-Instituto Butantan (HVB-IB) were studied: 411 of in 1983/84 (group A) and 319 in 1986 (group B). All the patients were seen in the Hospital 6 hours after the bite. As an average, all the 411 patients of the group A and the 319 patients of the group B received antivenom capable of neutralizing 215 mg and 117 mg of Bothrops jararaca, respectively. Both groups were similar concerning to: sex and age of the patients; anatomic region bitten; frequency of incision and tourniquet use at the site bite; time in between of the accident and the admission at HVB-IB; classification of B. jararaca either young or adult; frequency of the coagulation impairment. There was no difference in the evolution of the local envenoming manifestations and there were no cases of death.

Adolescent↗
PubMed1983

Biophysical properties and amino acid composition of Bothrops protease A, a proteolytic enzyme isolated from the venom of the snake Bothrops jararaca (jararaca).

Bothrops protease A, an arginine-ester hydrolase, is active on protamine, gelatin and insulin and was isolated from the venom of Bothrops jararaca in a homogeneous state, as judged by polyacrylamide gel electrophoresis and ultracentrifugal analyses. The enzyme has a molecular weight of 65,000 and a pI of 3.55. The enzyme is a glycoprotein whose amino acid content corresponds to 55% of the molecular weight.

Amino Acids↗
PubMed1990

Isolation of basic myotoxins from Bothrops moojeni and Bothrops atrox snake venoms.

Three myotoxins, one from the venom of Bothrops atrox and two from the venom of B. moojeni, were isolated by ion-exchange chromatography on CM-Sephadex C-25. The three toxins are basic proteins with an estimated mol. wt of about 13,500, and similar amino acid compositions. When injected into the gastrocnemius muscle of mice, the three toxins induce drastic myonecrosis of rapid onset, as judged by histological observation and quantitation of plasma creatine kinase levels. B. atrox myotoxin also has phosphlipase A2 and anticoagulant activities, whereas B. moojeni myotoxins I and II lack these effects. The three toxins are antigenically similar to each other, and to previously isolated myotoxins I and II from the venom of B. asper, when tested by gel immunodiffusion against rabbit antiserum to B. asper myotoxin I. Two monoclonal antibodies against B. asper myotoxins were tested against the newly purified proteins. MAb-3 recognizes all of them, whereas MAb-4 recognizes only B. atrox myotoxin, by enzyme-immunoassay. B. atrox and B. moojeni myotoxins can be tentatively classified within a group of myotoxins having phospholipase A2 structure present in Bothrops venoms.

Amino Acids↗
PubMed1992

Effect of a proteinase inhibitor from the plasma of Bothrops jararaca on coagulant and myotoxic activities of Bothrops venoms.

A proteinase inhibitor purified from the plasma of Bothrops jararaca was tested for the neutralization of total blood clotting activity, prothrombin activating factor and thrombin-like activity of B. jararaca venom and also myotoxic activity of B. jararacussu venom. This inhibitor was also tested for neutralization of the lethality induced by the venom of B. jararaca and B. jararacussu. The inhibitor markedly reduced the total blood clotting activity (95%) and the prothrombin activating factor (98%), and partially decreased the thrombin-like activity of B. jararaca venom. The proteinase inhibitor failed to neutralize the myotoxic activity of B. jararacussu. Lethality induced by the venom of B. jararaca in mice was inhibited by the proteinase inhibitor, whereas the protection on B. jararacussu venom was only partial. These results show that the proteinase inhibitor purified from the plasma of B. jararaca inhibits different proteinases but not myotoxins of Bothrops venoms, and consequently neutralizes the toxic effect due to these proteins.

Animals↗
PubMed2000

Neutralizing capacity of commercial bothropic antivenom against Bothrops jararacussu venom and bothropstoxin-I.

Bothrops jararacussu venom and its major toxin, bothropstoxin-I (BthTX-I), possess myotoxic and neurotoxic activities. The ability of commercial equine antivenom to neutralize these activities was studied in mouse isolated phrenic nerve-diaphragm (PND) and extensor digitorum longus (EDL) preparations by indirect stimulation (0.1 HZ, 0.2 ms). The time required to produce 50% neuromuscular blockade in the PND and EDL preparations was, respectively, 70 +/- 11.5 min and 58 +/- 8 min for B. jararacussu venom (50 microg/mL), and 31 +/- 6 min and 30 +/- 3 min for BthTX-I (20 microg/mL). After a 120-min incubation, the creatine kinase (CK) concentrations in the EDL preparations were 3464 +/- 346 U/L and 3422 +/- 135 U/L following exposure to venom (50 microg/mL) and BthTX-I (20 microg/mL), respectively. Antivenom neutralized the neuromuscular blockade induced by the venom and toxin in PND preparations in a dose-dependent fashion, but only partially neutralized this effect in EDL. Antivenom also effectively prevented the venom- and toxin-induced release of CK from EDL. In contrast, histological analysis showed that the morphological damage caused by B. jararacussu venom and BthTX-I in the EDL was only partially prevented by the anti- venom. These results indicate that commercial equine antiserum fully protects against the neurotoxic action of B. jararacussu and BthTX-I in PND preparations, but only partially protects against the neurotoxic and myotoxic actions of the venom and its toxin in EDL preparations. Care must therefore be exercized in extrapolating results from different preparations even when similar pharmacological or physiological responses are involved.

Animals↗
PubMed2000

Myotoxic phospholipases A(2) in bothrops snake venoms: effect of chemical modifications on the enzymatic and pharmacological properties of bothropstoxins from Bothrops jararacussu.

Venoms from eight Bothrops spp. were fractionated by ion-exchange chromatography on CM-Sepharose at pH 8.0 for the purification of myotoxins. Chromatographic profiles showed differences regarding myotoxic components among these venoms. B. alternatus, B. atrox and B. jararaca venoms did not show the major basic myotoxic fractions identified in the other venoms. Polyacrylamide gel electrophoresis for basic proteins also showed distinct patterns for these toxins. In vivo, all the isolated myotoxins induced release of creatine kinase due to necrosis of muscle fibers, accompanied by polymorphonuclear cell infiltration, and edema in the mouse paw. In addition, the toxins showed cytotoxic and liposome-disrupting activities in vitro. B. jararacussu bothropstoxins-I (BthTX-I) and II (BthTX-II) were submitted to chemical modifications of: His, by 4-bromophenacyl bromide (BPB) or photooxidation by Rose Bengal (RB); Tyr, by 2-nitrobenzenesulphonyl fluoride (NBSF); and Trp, by o-nitrophenylsulphenyl chloride (NPSC). The myotoxic and cytotoxic activities of BthTX-I, a Lys49 PLA(2) homologue, after modification by BPB, RB, NBSF and NPSC, were reduced to 50%, 20%, 75%, 65% and 13%, 0.5%, 76%, 58%, respectively. However, the edema-inducing and liposome-disrupting activities were not significantly reduced by the above modifications. BPB-treated BthTX-II, an Asp49 PLA(2) homologue, lost most of its catalytic, indirect hemolytic, anticoagulant, myotoxic and cytotoxic activities. The edema-inducing and liposome-disrupting activities were reduced to 50% and 80%, respectively. Lethality caused by BthTX-I and -II was strongly reduced after treatment with BPB or RB, but only partially with NBSF or NPSC. BthTX-I and -II, both native or modified, migrated similarly in a charge-shift electrophoresis. Antibodies raised against BthTX-I or -II, B. asper Basp-II and the C-terminal 115-129 peptide from Basp-II did not show significant differences in their cross-reactivity with the modified toxins, except with RB photooxidized toxins.

Animals↗
PubMed1993

Preparación toxoide a partir de la fracción hemorrágica del veneno de Bothrops asper (serpiente de América Central y del Sur) (Toxoid preparation from hemorrhagic fraction of the venom from Bothrops asper (snake from Central and South America).

A technique is described for preparing a toxoid from the hemorrhagic fraction of the Bothrops asper venom. This method conserves a high degree of immunogenicity although it eliminates lethal effects. None of the animals vaccinated with the toxoid from this fraction had hemorrhagic lesions after they were injected the venom from the hemorrhagic fraction.

Animals↗
PubMed1993

Crystallization and preliminary diffraction data of two myotoxins isolated from the venoms of Bothrops asper (Terciopelo) and Bothrops nummifer (jumping viper).

Two myotoxins isolated from B. asper (myotoxin II) and B. nummifer (myotoxin I) snake venoms have been crystallized and their diffraction properties are described. These myotoxins are phospholipase A2 variants which lack enzymatic activity; B. asper myotoxin II is a lysine-49 phospholipase. Crystals were obtained at room temperature by standard hanging-drop vapour diffusion methods. Crystals diffracted to a resolution of 2.8 and 2.3 A, respectively.

Animals↗
PubMed1997

Inhibition of proteases, myotoxins and phospholipases A2 from Bothrops venoms by the heteromeric protein complex of Didelphis albiventris opossum serum.

The antibothropic complex (ABC) from opossum (species Didelphis albiventris) serum was purified by chromatography on DEAE-Sephacel. It showed an acidic character and two polypeptide chains of ca. 45 kDa and 48 kDa, respectively. Lyophilized opossum serum or the ABC (100 micrograms), as well as ethylenediamine tetraacetate (0.25 mumoles) were able to completely neutralise the hemorrhagic effect of 50 micrograms of the desiccated venoms of Bothrops moojeni, Bothrops pirajai and Bothrops jararacussu. The myotoxic (100 micrograms venom in mice) and edematogenic (90 micrograms venom in rats) activities of Bothrops moojeni and Bothrops jararacussu venoms, as well as of the major myonecrotic protein (myotoxin-I) isolated from Bothrops moojeni venom, were also totally inhibited by the ABC (200 micrograms and 270 micrograms, respectively). The lyophilized opossum serum (30 micrograms) and the ABC (30 micrograms) reduced to 50% the phospholipase A2 activity of Bothrops moojeni venom (10 micrograms). The clotting activity of Bothrops alternatus and Bothrops moojeni (20 micrograms) on bovine plasma was also significantly inhibited by the ABC (60 micrograms).

Animals↗
PubMedDate not supplied

[Inefficacy of bothropic antivenin in the neutralization of the coagulation activity of Lachesis muta muta venom. Report of a case and experimental confirmation].

In the State of Amazonas and in areas nearby Manaus, the snakes responsible for the majority of accidents are Bothrops atrox and Lachesis muta muta, with a percentage of confirmed species of 76% and 17%, respectively. Frequently, in the absence of the laquetic and bothropic-laquetic antivenoms, the Instituto de Medicina Tropical de Manaus (IMTM) has been using bothropic antivenom in the treatment of laquetic accident. In this paper is related a case of accident caused by L. muta muta; the patient was treated with bothropic antivenom, and after received twenty ampoules of this antivenom, maintained blood incoagulability until the 13th day after the accident. Experiments to obtain the potency of the bothropic antivenom for the coagulant and hemorrhagic activities has been done, using Bothrops atrox venom as control. The results showed that the potency of the antivenom for the hemorrhagic activity was similar, and the potency for the coagulant activity for the L. m. muta venom was 9.2 times minor than that for B. atrox. The antibodies titles from three different lots of bothropic antivenom varied for the L. m. muta venom, and were constant for the B. atrox venom. Due to the inefficiency of the bothropic antivenom on the neutralization of the coagulant activity for the L. m. muta venom, the use of bothropic antivenom is not recommended in the treatment of Lachesis muta muta accidents.

Adult↗