A comparison of adhesive performance among six cursorial spider species

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  A comparison of adhesive performance among six cursorial spider species Abstract The ability to adhere to surfaces is particularly relevant for cursorial predatory arthropods like hunting spiders, which often traverse relatively complex environments characterized by large variation in substrate properties. Here, we evaluated the adhesive performance of six hunting spider species that are common in eastern temperate North America and lack specialized tarsi for climbing smooth or inclined surfaces [Lycosidae: Pardosa lapidicina Emerton, 1885 and Rabidosa rabida (Walckenaer, 1837); Oxyopidae: Oxyopes salticus Hentz, 1845; Pisauridae: Pisaurina mira (Walckenaer, 1837); Dolomedidae: Dolomedes triton (Walckenaer, 1837), and Dolomedes scriptus Hentz, 1845]. We tested adhesion performance as shear load resistance (g) on a glass plate, and as the angle of failure (°) when the plate was gradually inclined relative to horizontal. Average angle of failure and shear resistance differed among ...

Procoagulant Effects of Bothrops diporus Venom: Kinetic Modeling and Role of Serine Protease Activity

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Procoagulant Effects of Bothrops diporus Venom: Kinetic Modeling and Role of Serine Protease Activity

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 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.

Lopez, G. L., Nielsen, S. A., Nielsen, V. G., & Fusco, L. S. (2025). Procoagulant Effects of Bothrops diporus Venom: Kinetic Modeling and Role of Serine Protease Activity. International Journal of Molecular Sciences, 26(19), 9496. https://doi.org/10.3390/ijms26199496