Inter-individual variability in equine antibody responses to African snake venoms follows heavy-tailed distributions with implications for antivenom production

Posted by
  Inter-individual variability in equine antibody responses to African snake venoms follows heavy-tailed distributions with implications for antivenom production Abstract Variability in the antibody response of horses used for snake antivenom manufacture is well recognized, yet its statistical structure and implications for industrial productivity remain poorly characterized. In this study, we quantified antivenom antibody titers by ELISA in a cohort of 14 horses immunized with venoms from the clinically most important snakes in sub-Saharan Africa. To integrate antibody levels with plasma availability, we calculated the Cumulative Plasma Productivity (CPP) by converting individual plasma volumes into titer-corrected equivalents and sequentially pooling these volumes according to their corrected contribution. Distributional analysis revealed right-skewed, heavy-tailed patterns better approximated by a log-normal model than by a strict Pareto (power-law) form, with approximately 20–3...

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

Posted by

 


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