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Molecular Mechanisms of Venom and Antivenom

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Toxicology".

Deadline for manuscript submissions: 30 November 2025 | Viewed by 995

Special Issue Editor

Special Issue Information

Dear Colleagues,

Great strides have been made in the molecular characterization of venoms from reptiles and insects over the past few decades. Numerous methods, such as mass spectroscopy, electrophoresis, spectrophotometric enzymatic kinetic analyses, and viscoelastic analyses, have been employed both separately and in combination to define the molecular mechanisms and clinical relevance of whole venoms and their purified, isolated enzymatic agents. The next major advancement lies in integrating analytical techniques not only to determine the molecular characteristics of venom enzymes (e.g., amino acid sequence, molecular structure) but also to evaluate their impact on target systems, both in vitro and in live organisms. This Special Issue invites submissions that utilize molecular methods to characterize whole venoms and purified enzymes or other proteins, while also determining the effects of venom/purified proteins on target systems (e.g., coagulation system, neuromuscular junction) with in vitro or whole-animal models. Both original works or review articles are welcome.

Prof. Dr. Vance G. Nielsen
Guest Editor

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Keywords

  • venom
  • antivenom
  • mass spectroscopy
  • spectrophotometry
  • thromboelastography
  • coagulation
  • neuromuscular junction

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Published Papers (2 papers)

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Research

21 pages, 3094 KB  
Article
Comparative Proteomics, Functional Characterization and Immunological Cross-Reactivity Studies on Russell’s Viper Venom from Two Distinct Geographical Regions in South India
by Nisha Reghu, Sudharshan Rao, Dileepkumar Raveendran, Bipin Gopalakrishnan Nair and Muralidharan Vanuopadath
Int. J. Mol. Sci. 2025, 26(19), 9734; https://doi.org/10.3390/ijms26199734 - 7 Oct 2025
Viewed by 281
Abstract
Snakebite envenoming is a neglected tropical disease contributing to a significant number of morbidities and mortalities globally. Reports indicate that venom variation influences antivenom efficacy, which might affect treatment outcomes. The venom composition of Daboia russelii (Russell’s viper), one of the big four [...] Read more.
Snakebite envenoming is a neglected tropical disease contributing to a significant number of morbidities and mortalities globally. Reports indicate that venom variation influences antivenom efficacy, which might affect treatment outcomes. The venom composition of Daboia russelii (Russell’s viper), one of the big four snakes in India, has been extensively studied from different geographical regions of India. Nonetheless, the Russell’s viper venom proteome from Kerala (Western Ghats region), together with its study in comparison with the same species’ venom from Tamil Nadu, has not been explored yet. In the current study, Daboia russelii venom from Irula (RVi) and the Western Ghats region in Kerala (RVwg) was characterized through mass spectrometry-based proteomics and few functional assays. The proteomics study identified 52 proteins from 14 snake protein families in RVi and 61 proteins from 17 snake venom protein families in RVwg. Some of the protein families, including DNase and hyaluronidase, as well as vascular endothelial growth factor, were exclusively identified in RVwg venom. Comparative functional analysis indicated that RVwg exhibited higher fibrinogenolytic and hyaluronidase activities, while RVi venom showed higher phospholipase A2 and L-amino acid oxidase activities. Through ELISA, RVi venom showed an end-point titration value of 1:24,300 for all the antivenoms used in this study, whereas for RVwg, compared to PSAV (Premium serums and vaccines) (1:2700), Virchow and VINS (both 1:8100) antivenoms showed better immunological cross-reactivity. Immunoblotting experiments indicated differential binding and recognition of antigenic epitopes present in both venoms by the polyvalent antivenoms used in the current study. All these findings highlight that the venom proteome varies according to the geographical location, and this significantly influences antivenom efficacy. Full article
(This article belongs to the Special Issue Molecular Mechanisms of Venom and Antivenom)
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16 pages, 2588 KB  
Article
Procoagulant Effects of Bothrops diporus Venom: Kinetic Modeling and Role of Serine Protease Activity
by Gisela L. Lopez, Sarah A. Nielsen, Vance G. Nielsen and Luciano S. Fusco
Int. J. Mol. Sci. 2025, 26(19), 9496; https://doi.org/10.3390/ijms26199496 - 28 Sep 2025
Viewed by 313
Abstract
Bothrops species are responsible for the majority of envenomations in Argentina. In particular, Bothrops diporus is among the main species responsible for the majority of envenomations in Argentina and causes significant injury and coagulopathy. Given the significance of this venom, the authors sought [...] Read more.
Bothrops species are responsible for the majority of envenomations in Argentina. In particular, Bothrops diporus is among the main species responsible for the majority of envenomations in Argentina and causes significant injury and coagulopathy. Given the significance of this venom, the authors sought to define the toxin responsible for coagulopathy with specialized spectrophotometric and thromboelastographic methods. Utilizing clotting time, spectrophotometry, and thromboelastography, it was determined that B. diporus venom has potent, procoagulant activity in human plasma and buffer milieu. Calcium-dependent and -independent activities consistent with serine protease activity were identified. The activity included both thrombin-generating and thrombin-like enzymatic activity. The venom cleaved the serine protease-specific chromogenic substrate β-Ala-Gly-Arg-p-nitroanilide diacetate, and its activity was inhibited in plasma by antithrombin after addition of heparin. Further, venom exposed in isolation to RuCl3, a known inhibitor of serine protease-containing venoms, demonstrated decreased activity in human plasma. In conclusion, the present study contributes to a better understanding of B. diporus venom and may have implications for the rational design of inhibitors, antivenom formulations, or preclinical models to study venom-induced coagulopathies. Full article
(This article belongs to the Special Issue Molecular Mechanisms of Venom and Antivenom)
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