Transcriptomic Insights Into the Evolution of Snake Venom: Mechanisms, Diversity, and Adaptation

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  Transcriptomic Insights Into the Evolution of Snake Venom: Mechanisms, Diversity, and Adaptation Abstract Snake venoms are evolutionarily refined biochemical arsenals composed of diverse toxins with complex functional roles in predation, defense, and competition. Over the past 2 decades, transcriptomic approaches have transformed venom research by enabling high-resolution insights into gene expression dynamics, molecular diversity, and the evolutionary mechanisms driving venom variation across lineages. In this review, we present a comprehensive synthesis of snake venom transcriptomics literature and propose a conceptual framework structured around three major axes: (1) gene family expansion through duplication and neofunctionalization; (2) regulatory complexity encompassing transcriptional, posttranscriptional, and epigenetic modulation; and (3) ecological selection pressures shaping venom profiles in response to diet, habitat, and interspecific interactions. We integrate findin...

Inhibition of Chikungunya virus nsP2 protease in vitro by scorpion venom peptide pantinin-1

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Inhibition of Chikungunya virus nsP2 protease in vitro by scorpion venom peptide pantinin-1

Abstract

Climate change has facilitated the spread of arboviruses like the Chikungunya virus (CHIKV). CHIKV, a re-emerging virus from the Togaviridae family, has caused numerous global outbreaks. The absence of antiviral therapy against CHIKV poses a significant threat to public health. The cleavage of the viral polyprotein relies on the catalytic activity of nsP2, crucial for viral replication. Therefore the nsP2 protease presents a promising target for antiviral drug development. Animal venom-derived peptides demonstrated potential in combating various diseases including infections, cancer, and neurodegenerative disorders. In this study, we assessed the inhibitory effects of pantinin-1, a peptide derived from the scorpion Pandinus imperator with broad antimicrobial activity, against CHIKV nsP2 protease. Pantinin-1 effectively inhibited CHIKV nsP2 protease, with a half-maximal inhibitory concentration (IC₅₀) of 6.4 ± 2.04 µM and complete inhibition at 175 µM. Further examination revealed that pantinin-1 functions as a competitive inhibitor with low micromolar affinity and exhibited no toxicity up to 20 µM in cell culture. Using docking and molecular dynamics simulations, the protein-peptide interaction was analyzed, and the key residues involved in the protease binding were predicted. These findings underscore the potential of pantinin-1 as a lead candidate targeting nsP2 protease.

Mastalipour, M., Coronado, M. A., Hernández González, J. E., Willbold, D., & Eberle, R. J. (2026). Inhibition of Chikungunya virus nsP2 protease in vitro by scorpion venom peptide pantinin-1. PLOS ONE, 21(4), e0346930. https://doi.org/10.1371/journal.pone.0346930