Neutralization of Vipera and Macrovipera venoms by two experimental polyvalent antisera: A study of paraspecificity

Archundia, Irving G.; Roodt, Adolfo Rafael de; Ramos‐Cerrillo, Blanca; Chippaux, Jean-Philippe; Olguín-Pérez, Laura; Alagón, Alejandro; Stock, Roberto P.

doi:10.1016/j.toxicon.2011.04.009

Cited by 30 publications

(28 citation statements)

References 40 publications

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“…From the immunization protocols described by our group [ 11 , 12 ] together with those reported by El-Kady et al [ 13 ] and Archundia et al [ 14 ], the common features which have led to the production of potent antisera are as follows:…”

Section: Discussionmentioning

confidence: 99%

“…El-Kady et al [ 13 ] showed that the significant improvement in potency achieved by this protocol was due to the production of specific antibodies against the venom toxins/proteins that prossessed high affinity. A low venom dose, complete Freund’s adjuvant and incomplete Freund’s adjuvant (CFA/IFA) immunization protocol was shown to successfully produce potent polyspecific antisera against viperid venoms [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

“…The selection of a monospecific antivenom for treatment is based on identification of the culprit snake and on the signs and symptoms present in patients after snakebite. When the identification of the envenoming species is not certain, it is better to use a polyspecific antivenom that is effective against venoms of several species of snakes present in the area [ 14 , 15 ]. The aim of the present study was to use a ‘low dose low volume, multi-site’ immunization strategy which had been shown to be highly effective with elapid (cobra and kraits) venoms [ 11 , 12 ], to produce potent polyspecific antisera against the three medically important vipers ( Calloselasma rhodostoma , Cryptelytrops albolabris and Daboia siamensis ) of Thailand and its neighboring countries while at the same time causing minimal side-effects on the horses.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effective Equine Immunization Protocol for Production of Potent Poly-specific Antisera against Calloselasma rhodostoma, Cryptelytrops albolabris and Daboia siamensis

et al. 2015

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Snake envenomation has been estimated to affect 1.8 million people annually with about 94,000 deaths mostly in poor tropical countries. Specific antivenoms are the only rational and effective therapy for these cases. Efforts are being made to produce effective, affordable and sufficient antivenoms for these victims. The immunization process, which has rarely been described in detail, is one step that needs to be rigorously studied and improved especially with regard to the production of polyspecific antisera. The polyspecific nature of therapeutic antivenom could obviate the need to identify the culprit snake species. The aim of this study was to produce potent polyspecific antisera against 3 medically important vipers of Thailand and its neighboring countries, namely Cryptelytrops albolabris "White lipped pit viper" (CA), Calleoselasma rhodostoma “Malayan pit viper” (CR), and Daboia siamensis “Russell’s viper” (DS). Four horses were immunized with a mixture of the 3 viper venoms using the ‘low dose, low volume multi-site’ immunization protocol. The antisera showed rapid rise in ELISA titers against the 3 venoms and reached plateau at about the 8th week post-immunization. The in vivo neutralization potency (P) of the antisera against CA, CR and DS venoms was 10.40, 2.42 and 0.76 mg/ml, respectively and was much higher than the minimal potency limits set by Queen Soavabha Memorial Institute (QSMI). The corresponding potency values for the QSMI monospecific antisera against CA, CR and DS venoms were 7.28, 3.12 and 1.50 mg/ml, respectively. The polyspecific antisera also effectively neutralized the procoagulant, hemorrhagic, necrotic and nephrotoxic activities of the viper venoms. This effective immunization protocol should be useful in the production of potent polyspecific antisera against snake venoms, and equine antisera against tetanus, diphtheria or rabies.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Effective Equine Immunization Protocol for Production of Potent Poly-specific Antisera against Calloselasma rhodostoma, Cryptelytrops albolabris and Daboia siamensis

et al. 2015

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“…The median lethal dose (LD 50 ) of MLO venom for intravenous injection (IV) was determined previously by two different groups. Archundia and coworkers in 2011 determine the LD 50 of MLO venom to be 30.1 µg/mouse [22] , whereas Kurtović et al [23] found LD 50 to be 18.4 µg/mouse. Considering this discrepancy and the absence of data on the IP route of venom administration in rats, we have tested and established toxicity (LD 50 ) for IP injection of MLO venom for mice and rats.…”

Section: Toxicological Investigationsmentioning

confidence: 99%

Changes in microglia activity of rat brain induced by Macrovipera lebetina obtusa venom

Darbinyan¹,

Antonyan²,

Koshatashyan³

et al. 2018

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Aims: The microglia activity of rat brain following exposure of the Macrovipera lebetina obtusa venom was investigated. Methods: Histochemical analysis of brain microcirculatory bed staining by Ca 2+ ATPase method for variable doses after intraperitoneal injections given for different time periods was used. The hemorrhagic activity of snake venom metalloproteinases was tested. Toxicological data were calculated using Behrens and Miller-Tainter methods. Surface, size of brain microglial cells (MGCs) and staining intensity were quantified using ImageJ software. Results: The vasodestructive action of the venom resulted in changes in ATPase activity. The intensity of staining of rat brain microcirculatory bed was venom dose-, and time-dependent. Increased activity of MGCs in hemorrhagic loci of different regions of venom affected brain was also demonstrated. Conclusion: The activation of microglia and changes of its form, size, and position strongly correlates with hemorrhage-induced cerebrovascular damage.

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“…To date, however, a little is known about the proteases in their venom. As regards the M. deserti and M. lebetina, to the best of our knowledge, there are only two studies availabe which have examined their venom; one study examined the hemorrhagic, necrotizing and inflammatoryedematogenic activity (13), and the other surveyed para-specific neutralization against the venom using a polyvalent serum (14). M. lebetina venom, however, has been relatively well documented (15)(16)(17).…”

Section: Introductionmentioning

confidence: 99%

Purification and biochemical characterization of a fibrin(ogen)olytic metalloprotease from Macrovipera mauritanica snake venom which induces vascular permeability

Lee

Park

et al. 2014

International Journal of Molecular Medicine

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In the present study, a novel fibrin(ogen)olytic metalloprotease from Macrovipera mauritanica snake venom was purified and characterized in terms of enzyme kinetics and substrate specificity. The purified enzyme [termed snake venom metalloprotease-Macrovipera mauritanica (SVMP‑MM)] was composed of a single polypeptide with an apparent molecular weight of 27 kDa, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The N-terminus of the enzyme was composed of NH(2)-QRFAPRYIEL-COOH, as determined by N-terminal sequencing. The Aα- and the Bβ-chains of fibrinogen were completely cleaved by SVMP-MM within 20 and 480 min, respectively. However, the γ-chain was much more resistant to digestion by the enzyme. The enzyme also exhibited proteolytic activity, cleaving the α-α polymer of cross-linked fibrin, but did not effectively digest the γ-γ polymer. To determine the kinetic parameters for SVMP-MM, a fluorescence-quenching peptide (termed o-aminobenzoic acid-HTEKLVTS-2,4-dinitrophenyl‑NH(2)) containing a K-L sequence for SVMP-MM cleavage was designed and synthesized. The optimal pH and temperature for the enzyme activity were found to be 5.5 and 37˚C, respectively, when the fluorogenic substrate was synthesized and used as a substrate. Among the various divalent cations tested, Ni(2+) and Cu(2+) showed strong inhibitory effects on enzyme activity, with an average of 69.6% inhibition. The enzyme activity was also inhibited by treatment with 1,10-phenanthroline, ethylenediaminetetraacetic acid and glycol-bis-(2‑aminoethylether)-N,N,N',N'-tetra-acetic acid, but not with aprotinin, tosyl-lysine chloromethyl ketone and tosyl-phenylalanyl chloromethyl ketone, suggesting that SVMP-MM is a metalloprotease and not a serine protease. The enzymatic parameters, including the K(M), k(cat), and k(cat)/K(M) values were estimated to be 0.015 mM, 0.031 sec(-1), and 20.67 mM(-1)sec(-1), respectively. SVMP-MM induced vascular permeability by digesting type IV collagen. The results obtained in our study demonstrate that SVMP-MM is a fibrin(ogen)olytic P-I class metalloprotease, which can induce a hemorrhagic reaction in vivo.

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Neutralization of Vipera and Macrovipera venoms by two experimental polyvalent antisera: A study of paraspecificity

Cited by 30 publications

References 40 publications

Effective Equine Immunization Protocol for Production of Potent Poly-specific Antisera against Calloselasma rhodostoma, Cryptelytrops albolabris and Daboia siamensis

Effective Equine Immunization Protocol for Production of Potent Poly-specific Antisera against Calloselasma rhodostoma, Cryptelytrops albolabris and Daboia siamensis

Changes in microglia activity of rat brain induced by Macrovipera lebetina obtusa venom

Purification and biochemical characterization of a fibrin(ogen)olytic metalloprotease from Macrovipera mauritanica snake venom which induces vascular permeability

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