Venom composition of the Iberian adder (Vipera seoanei) from northern Portugal reveals limited sex and size variation

Posted by
  Venom composition of the Iberian adder (Vipera seoanei) from northern Portugal reveals limited sex and size variation Abstract Snake venom is a complex and dynamic ecological trait, with high potential for intraspecific variation. In this study, the venom composition of the Iberian adder ( Vipera seoanei ) from the Peneda Mountains of northern Portugal was investigated to explore whether venom varies with body size and sex. Venom proteomes from six individuals representing juvenile, subadult, and adult males and females were characterised using LC–MS/MS, while individual variation was assessed from SDS–PAGE profiles of 18 snakes. LC–MS/MS identified 144 proteins, dominated by phospholipases A 2 (PLA 2 ), snake venom serine proteases (svSP), and C-type lectin-related proteins (CTL). Descriptive comparisons revealed contrasting individual profiles, particularly between the juvenile male, characterised by high svSP and svMP abundance, and the juvenile female, characterised by high ...

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

Posted by

 


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