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 ...

Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom

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Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom

Abstract

Venom plays a crucial role in the defense and predation of venomous animals. Spiders (Araneae) are among the most successful predators and have a fascinating venom composition. Their venom mainly contains disulfide-rich peptides and large proteins. Here, we analyzed spider venom protein families, utilizing transcriptomic and genomic data, and highlighted their similarities and differences. We show that spiders have specific combinations of toxins for better predation and defense, typically comprising a core toxin expressed alongside several auxiliary toxins. Among them, the CAP superfamily is widely distributed and highly expressed in web-building Araneoidea spiders. Our analysis of evolutionary relationships revealed four subfamilies (subA-subD) of the CAP superfamily that differ in structure and potential functions. CAP proteins are composed of a conserved CAP domain and diverse C-terminal domains. CAP subC shares similar domains with the snake ion channel regulator svCRISP proteins, while CAP subD possesses a sequence similar to that of insect venom allergen 5 (Ag5). Furthermore, we show that gene duplication and selective expression lead to increased expression of CAP subD, making it a core member of the CAP superfamily. This study sheds light on the functional diversity of CAP subfamilies and their evolutionary history, which has important implications for fully understanding the composition of spider venom proteins and the core toxin components of web-building spiders.

Jiang, Hongcen, Yiru Wang, Guoqing Zhang, Anqiang Jia, Zhaoyuan Wei, and Yi Wang. 2024. "Identification and Evolutionary Analysis of the Widely Distributed CAP Superfamily in Spider Venom" Toxins 16, no. 6: 240. https://doi.org/10.3390/toxins16060240