Purification and partial characterization of a haemorrhagin (VRH-1) from Vipera russelli russelli venom

Chakrabarty, Dibakar; Bhattacharyya, Debasish; Sarkar, Himadri Sekhar; Lahiri, Sites C.

doi:10.1016/0041-0101(93)90344-i

Cited by 30 publications

(18 citation statements)

References 12 publications

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“…Chicken IgY, lacking the evocative function on the mammalian complement system or Fc receptor, has been reported as passive immunization for clinical and experimental treatments (11)(12)(13)(14). Additional advantages of using chickens include inexpensive rearing, the high yield of IgY antibodies (ϳ100 to ϳ150 mg per egg), and a strong immune response elicited by a small amount of antigen, which is most beneficial when collection of venom proteins is difficult (15,16). Thus, hens supply a more hygienic, convenient, and costeffective platform to generate neutralizing antibodies against snake envenomation than horses (14,17).…”

Section: Importancementioning

confidence: 99%

Production and Characterization of Neutralizing Antibodies against Bungarus multicinctus Snake Venom

Lee

Leu

et al. 2016

Appl Environ Microbiol

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The venom of the banded krait (Bungarus multicinctus), one of the major venomous species in Taiwan, contains neurotoxic venom proteins (B. multicinctus proteins) that pose a serious medical problem in tropical and subtropical countries. Even though horse-derived serum is an efficient therapy against snake venom, it is associated with a high cost and side effects. Therefore, developing a more cost-effective alternative treatment option is highly envisaged. In this study, chickens were immunized with B. multicinctus proteins, and polyclonal immunoglobulin Y (IgY) antibodies were purified from eggs. IgY showed a binding activity to B. multicinctus proteins that was similar to horse antivenin, and its titer in chickens lasted for at least 6 months. We constructed two antibody libraries by phage display antibody technology, which contain 1.0 ؋ 10 7 and 2.9 ؋ 10 8 transformants, respectively. After biopanning, a phage-based enzyme-linked immunosorbent assay (ELISA) indicated that specific clones were enriched. Thirty randomly selected clones expressing monoclonal single-chain variable-fragment (scFv) antibodies were classified into four groups with a short linker and two with a long linker. These selected scFv antibodies showed specific binding activities to B. multicinctus proteins but not to the venomous proteins of other snakes. Most importantly, polyclonal IgY demonstrated a similar neutralization efficiency as did horse-derived antivenin in mice that were injected with a minimum lethal dosage (MLD) of venom proteins. A mixture of several monoclonal anti-B. multicinctus scFv antibodies was also able to partially inhibit the lethal effect on mice. We profoundly believe that IgY and scFv antibodies can be applied in developing diagnostic agents for wound exudates and as an alternative treatment for snakebite envenomation in the future. IMPORTANCESnake envenomation is one of the global medical issues of concern. Horse-derived antivenin is an effective way to treat snakebites, but it is costly and occasionally causes severe side effects. In this study, we first generated and characterized IgY antibodies with neutralization activity in chickens. Subsequently, we generated a panel of monoclonal scFv antibodies using phage display antibody technology. A mixture of scFv antibodies was able to partially inhibit the lethal effect in mice that were injected with lethal dosages of venom proteins and prolong their survival time. We believe that chicken-derived IgY and scFv antibodies have great potential for the development of diagnostic agents for wound exudates and therapeutic agents against snake envenomation in the future.

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Section: Importancementioning

confidence: 99%

Production and Characterization of Neutralizing Antibodies against Bungarus multicinctus Snake Venom

Lee

Leu

et al. 2016

Appl Environ Microbiol

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“…VRH-1 is identified to be a Mg 2+ containing metalloproteinase which shows organ-specific hemorrhagic property (Chakrabarty et al 1993). Structurally, VRH-1 has been suggested to be a globular protein of a single polypeptide chain of 22 kDa which is not asymmetric in shape (Chakrabarty et al 1993). However, further structural details of VRH-1 have not been elucidated till date.…”

Section: Vrh-1mentioning

confidence: 97%

“…However, further structural details of VRH-1 have not been elucidated till date. This hemorrhagic metalloproteinase was reported to be devoid of esterase activity and does not affect the process of blood coagulation (Chakrabarty et al 1993). Though the complete characterization of VRH-1 as well as studies pertaining to its neutralization by RV antivenom is still warranted, the contribution of VRH-1 to the overall hemorrhagic effect of RVV cannot be neglected.…”

Section: Vrh-1mentioning

confidence: 98%

“…Snake venom metalloproteinases (SVMPs) play a significant role in venom-induced pathogenesis by damaging the local tissues and causing tissue necrosis (Chakrabarty et al 1993(Chakrabarty et al , 2000Mukherjee 2008;Chen et al 2008). Structurally, SVMPs are monozinc endopeptidases that are classified under the subfamily of "reprolysins" along with the ADAMs ("a disintegrin and metalloproteinase" proteins) (Bode et al 1993;Hite et al 1994;Gutierrez and Rucavado 2000;Fox and Serrano 2009), as they share a common overall domain organization (Hite et al 1994;Moura-da-Silva et al 2011).…”

Section: Rvv Metalloproteinasesmentioning

confidence: 99%

“…Yet another proteinase contributing to the overall toxic effects of RV envenomation is VRH-1 (Chakrabarty et al 1993). VRH-1 is identified to be a Mg 2+ containing metalloproteinase which shows organ-specific hemorrhagic property (Chakrabarty et al 1993).…”

Section: Vrh-1mentioning

confidence: 99%

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A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases

Thakur

Mukherjee

2015

Snake Venoms

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Russell's viper (Daboia russelii) is an important member of the Viperidae family which is widely distributed across Southern Asia including India. Russell's viper venom (RVV) is indisputably a potent mixture of various toxic and nontoxic components that have evolved to interfere with vital physiological processes like coagulation and fibrinolysis. Many of these components are metallo-or serine proteinases. Venoms from the snakes of Viperidae family are reported to be rich in proteinases which contributes to hemostatic alterations in the victims and is also responsible for tissue-specific hemorrhagic effects. However, till date, not many proteinases have been reported from RVV. In this brief review, the currently available data on the structural and functional attributes of RVV proteinases have been focused and summarized. The pathophysiological significance and the therapeutic/ diagnostic application(s) of the identified RVV proteinases have also been discussed. It is relevant to note that a more detailed analysis of the entire complexity of RVV proteinases will contribute to the better understanding of their role in Russell's viper envenomation and subsequent antivenom therapy. Most importantly, novel RVV proteinases can also be explored for their usefulness in the development of diagnostic/therapeutic agents to deal with life-threatening diseases.

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A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases

Thakur¹,

Mukherjee²

2017

Snake Venoms

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Purification and partial characterization of a haemorrhagin (VRH-1) from Vipera russelli russelli venom

Cited by 30 publications

References 12 publications

Production and Characterization of Neutralizing Antibodies against Bungarus multicinctus Snake Venom

Production and Characterization of Neutralizing Antibodies against Bungarus multicinctus Snake Venom

A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases

A Brief Appraisal on Russell’s Viper Venom (Daboia russelii russelii) Proteinases

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