Evidence of venom variability associated with venom extraction interval in the monocled cobra (Naja kaouthia)

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  Evidence of venom variability associated with venom extraction interval in the monocled cobra (Naja kaouthia) Abstract Snake venom variability is a critical factor in antivenom production. Although several influencing factors have been studied, the impact of extraction interval on venom properties remains poorly understood. This study evaluated the effects of various extraction intervals on venom yield, the percentage of dry weight (%Dw), and composition in the monocled cobra ( Naja kaouthia ). Twenty-five captive snakes were randomly allocated to five groups, each undergoing a control extraction followed by a repeated extraction at 1, 4, 7, 10, or 14 days. Venom profiles were characterized using reversed-phase high-performance liquid chromatography (RP-HPLC) and Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS). Results indicated that while fresh venom yield remained stable across all intervals, %Dw significantly decreased in extractions performed between 1 and 10 days, ...

Toxic Peptides from the Mexican Scorpion Centruroides villegasi: Chemical Structure and Evaluation of Recognition by Human Single-Chain Antibodies

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Toxic Peptides from the Mexican Scorpion Centruroides villegasi: Chemical Structure and Evaluation of Recognition by Human Single-Chain Antibodies

Abstract

Alternative recombinant sources of antivenoms have been successfully generated. The application of such strategies requires the characterization of the venoms for the development of specific neutralizing molecules against the toxic components. Five toxic peptides to mammals from the Mexican scorpion Centruroides villegasi were isolated by chromatographic procedures by means of gel filtration on Sephadex G-50, followed by ion-exchange columns on carboxy-methyl-cellulose (CMC) resins and finally purified by high-performance chromatography (HPLC) columns. Their primary structures were determined by Edman degradation. They contain 66 amino acids and are maintained well packed by four disulfide bridges, with molecular mass from 7511.3 to 7750.1 Da. They are all relatively toxic and deadly to mice and show high sequence identity with known peptides that are specific modifiers of the gating mechanisms of Na+ ion channels of type beta-toxin (β-ScTx). They were named Cv1 to Cv5 and used to test their recognition by single-chain variable fragments (scFv) of antibodies, using surface plasmon resonance. Three different scFvs generated in our laboratory (10FG2, HV, LR) were tested for recognizing the various new peptides described here, paving the way for the development of a novel type of scorpion antivenom.

Riaño-Umbarila, Lidia, Timoteo Olamendi-Portugal, José Alberto Romero-Moreno, Gustavo Delgado-Prudencio, Fernando Z. Zamudio, Baltazar Becerril, and Lourival D. Possani. 2024. "Toxic Peptides from the Mexican Scorpion Centruroides villegasi: Chemical Structure and Evaluation of Recognition by Human Single-Chain Antibodies" Toxins 16, no. 7: 301. https://doi.org/10.3390/toxins16070301