Transcriptomic Insights Into the Evolution of Snake Venom: Mechanisms, Diversity, and Adaptation

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  Transcriptomic Insights Into the Evolution of Snake Venom: Mechanisms, Diversity, and Adaptation Abstract Snake venoms are evolutionarily refined biochemical arsenals composed of diverse toxins with complex functional roles in predation, defense, and competition. Over the past 2 decades, transcriptomic approaches have transformed venom research by enabling high-resolution insights into gene expression dynamics, molecular diversity, and the evolutionary mechanisms driving venom variation across lineages. In this review, we present a comprehensive synthesis of snake venom transcriptomics literature and propose a conceptual framework structured around three major axes: (1) gene family expansion through duplication and neofunctionalization; (2) regulatory complexity encompassing transcriptional, posttranscriptional, and epigenetic modulation; and (3) ecological selection pressures shaping venom profiles in response to diet, habitat, and interspecific interactions. We integrate findin...

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