A comparison of adhesive performance among six cursorial spider species

  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 ...

Venom Peptides Across Asian and American Tarantulas Utilize Dual Pharmacology to Target Activation and Fast Inactivation of Voltage-Gated Sodium Channels

 


Venom Peptides Across Asian and American Tarantulas Utilize Dual Pharmacology to Target Activation and Fast Inactivation of Voltage-Gated Sodium Channels

Abstract

Spider-derived venoms are a rich source of cystine knot peptides with immense therapeutic potential. Many of these peptides exert unique biological activities through the modulation of ion channels, including of human voltage-gated sodium (NaV1.1–NaV1.9) channels. NaV channel subtypes have diverse functions determined by their tissue and cellular distribution and biophysical properties, and are pathophysiology mediators in various diseases. Therefore, NaVs are central in studies of human biology. This work investigated the pharmacological properties of venom of the Thai theraphosid Ornithoctonus aureotibialis on NaV channels. We discovered a predominant venom peptide named Oa1a and assessed its pharmacological properties across human NaV channel subtypes. Synthetic forms of the peptide Oa1a showed preferential inhibition of NaV1.1 and NaV1.7, while recombinant Oa1a displayed a preference for inhibiting NaV1.2, NaV1.6, and NaV1.7. Interestingly, all versions of Oa1a peptides exerted dual pharmacological effect by reducing the peak current and slowing fast inactivation of NaV1.3, consistent with Oa1a having more than one binding site on NaV channels. Such complex pharmacology was previously observed for a venom peptide in a Central American and Costa Rican tarantula, suggesting a conserved mechanism of action amongst these geographically distinct species. However, Oa1a lacked activity in the T-type channels observed in the tarantula peptide from Central America. Structure–function relationships investigated using molecular modelling showed that the dual pharmacology is driven by a conserved mechanism utilizing a mix of aromatic and charged residues, while the T-type activity appears to require additional charged residues in loop 2 and fewer positive charges in loop 4. Future structure–activity relationship studies of Oa1a will guide the development of pharmacological tools as well as next-generation drugs to treat NaV channel dysfunction associated with neurological disorders.

Nashikwala, A. S., Kotapati, C., Eagles, D. A., Lewis, R. J., & Cardoso, F. C. (2025). Venom Peptides Across Asian and American Tarantulas Utilize Dual Pharmacology to Target Activation and Fast Inactivation of Voltage-Gated Sodium Channels. Toxins, 17(11), 561. https://doi.org/10.3390/toxins17110561