Sex Role–Dependent Behavioral and Architectural Divergence in a Jumping Spider

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  Sex Role–Dependent Behavioral and Architectural Divergence in a Jumping Spider ABSTRACT Sex differences in behavior and functional traits are often attributed to differences in mating effort intensity, but the role of sex-specific parental demands remains poorly understood. Using the jumping spider Toxeus maxillosus —where males engage in mate searching and courtship without providing parental care, while females provide extended maternal care from egg attendance to offspring maturity (around 3 months)—we conducted an exploratory investigation into whether these distinct selective pressures led to divergence in spatial behaviors and nest architecture. Results revealed that males and females showed equivalent accuracy, latency, and learning-related performance in both a route-planning test under water stress and a color-pattern associative memory task. In contrast, during nest-construction assays, females built complex, multi-entrance structures that closely matched the container'...

Conserved Enzymatic Peptides in Bitis arietans Venom Revealed by Comparative Proteomics: Implications for Cross-Reactive Antibody Targeting

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Conserved Enzymatic Peptides in Bitis arietans Venom Revealed by Comparative Proteomics: Implications for Cross-Reactive Antibody Targeting

Abstract

Snakebite envenoming remains a critical public health issue, and the molecular variability of venoms limits the cross-species efficacy of conventional antivenoms. Here, we conducted a comparative proteomic analysis of Bitis arietans venom to identify conserved peptide regions derived from enzymatic toxins and evaluate their potential relevance for complementary immunotherapeutic applications. Enzyme-enriched venom fractions were isolated through sequential affinity and ion-exchange chromatography and were subsequently characterized using fluorogenic FRET substrates and inhibitor assays. LC–MS/MS analysis identified 1099 proteins and revealed 36 conserved peptides within snake venom metalloproteinases (SVMPs), serine proteases (SVSPs), and phospholipase A2 (PLA2), particularly located near catalytic residues and structurally essential motifs such as the HExxHxxGxxH zinc-binding site in SVMPs, the His-Asp-Ser catalytic triad in SVSPs, and the Ca2+-binding loop in PLA2, across Viperidae venoms. These conserved regions were also observed in homologous toxin isoforms from additional Viperidae genera, supporting the evolutionary conservation of key functional domains. While sequence conservation alone does not guarantee neutralization capacity, the identified regions represent strong candidates for structural epitope mapping and targeted antibody development. This study provides a peptide-level framework for advancing complementary antibody-based therapies designed to broaden cross-species toxin recognition, reduce antivenom dosage requirements, and improve clinical outcomes in snakebite envenoming.

Godoi, K. S., Portaro, F. C., Spencer, P. J., Vigerelli, H., & Silva, W. D. (2026). Conserved Enzymatic Peptides in Bitis arietans Venom Revealed by Comparative Proteomics: Implications for Cross-Reactive Antibody Targeting. International Journal of Molecular Sciences, 27(3), 1431. https://doi.org/10.3390/ijms27031431