What’s a Spider? Designation of the Neotype for the First Animal Species Ever Described, Araneus angulatus Clerck 1757 (Araneae: Araneidae)

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  What’s a Spider? Designation of the Neotype for the First Animal Species Ever Described, Araneus angulatus Clerck 1757 (Araneae: Araneidae) Abstract We designate a neotype for the Eurasian spider species Araneus angulatus Clerck, 1757, thereby fixing the objective application of the species name, the genus name Araneus Clerck 1757, the family name Araneidae Clerck 1757, and the superfamily name Araneoidea Clerck 1757. By etymology and arachnological tradition, it also unofficially fixes the application of the ordinal name Araneae Clerck 1757 and thus answers the uncontroversial question, “What’s a spider?” A. angulatus also happens to be historically the first animal species ever described because Clerck (1757) has priority over Linnaeus (1758). Neotype designation is justified for three reasons: the syntypes of A. angulatus are lost; “ A. angulatus ” contains significant COI sequence divergence, potentially representing intraspecific variation, misidentifications, or as many...

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