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

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  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 ...

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