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 ...

Mass spectrometric analysis of Odonthobuthus Doriae scorpion venom and its non-neutralized fractions after interaction with commercial antivenom

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Mass spectrometric analysis of Odonthobuthus Doriae scorpion venom and its non-neutralized fractions after interaction with commercial antivenom

Abstract

It is believed that antivenoms play a crucial role in neutralizing venoms. However, uncontrolled clinical effects appear in patients stung by scorpions after the injection of antivenom. In this research, non-neutralized components of the venom of the Iranian scorpion Odonthobuthus doriae were analyzed after interacting with the commercial antivenom available in the market. The venom and antivenom interaction was performed, then centrifuged, and the supernatant was analyzed by high-performance liquid chromatography (HPLC). Two peaks of Odonthobuthus doriae venom were observed in the chromatogram of the supernatant. Two components were isolated by HPLC and analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) instruments. Peptide sequencing was done by Liquid Chromatography Quadrupole Time-of-Flight Tandem Mass Spectrometry (LC-Q-TOF MS/MS). Results indicate that the components of scorpion venom mainly have a molecular weight below 10 kDa, consisting of toxic peptides that disrupt the function of sodium and potassium channels. The MALDI-TOF MS results show that two toxic peptides with molecular masses of 6941 Da and 6396 Da were not neutralized by the antivenom. According to the MS/MS sequencing data, the components have been related to peptides A0A5P8U2Q6_MESEU and A0A0U4FP89_ODODO, which belong to the sodium and potassium channels toxins family, respectively.


Abdollahnia, A., Bahmani, K., Aliahmadi, A. et al. Mass spectrometric analysis of Odonthobuthus Doriae scorpion venom and its non-neutralized fractions after interaction with commercial antivenom. Sci Rep 14, 10389 (2024). https://doi.org/10.1038/s41598-024-59150-z