New locality records and future habitat suitability of Sassanidotus gracilis (Birula, 1900) (Scorpiones: Buthidae) in the Iran–Afghanistan–Pakistan arid belt

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  New locality records and future habitat suitability of Sassanidotus gracilis (Birula, 1900) (Scorpiones: Buthidae) in the Iran–Afghanistan–Pakistan arid belt Abstract This study reports new locality records from Iran and a climate-based habitat suitability assessment for Sassanidotus gracilis (Birula, 1900) (Scorpiones: Buthidae) in the Iran–Afghanistan–Pakistan arid belt. We document new specimens from Sistan and Baluchestan Province, Iran, with an updated distribution map and illustrations, and we model the species' potential distribution across south-eastern Iran and adjacent parts of Afghanistan and Pakistan. Habitat suitability was associated mainly with precipitation seasonality, precipitation of the wettest month, precipitation of the driest month, and slope. In an arid setting these rainfall variables are unlikely to indicate a need for moist habitat; they more plausibly track seasonal productivity and the terrain features that provide shelter. Present-day suitable areas...

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