Comparative proteomic characterization of web silk toxins between two species of orb-weaving spiders Trichonephila clavipes and Nephilingis cruentata.

The silk strands spun by Nephilinae spiders are known to encompass a diverse array of peptidic and proteinaceous toxins, alongside low-molecular-weight toxins. This study employs a mass spectrometry-based proteomics methodology to comparatively assess the abundance of web silk toxins in two species of orb-weaving spiders, Trichonephila clavipes and Nephilingis cruentata. Results derived from the proteomic analysis revealed the presence of 54 proteinaceous toxin-like compounds on the web of N. cruentata and 63 counterparts in that of T. clavipes. Additionally, a set of 24 toxin-like proteins is identified as common between the webs of the two orb-weaving spider species. Functional enrichment analysis revealed that most proteins present in both webs are categorized as "toxins from the webs". This finding emphasizes the toxicological significance of these spider webs. Furthermore, insect toxicity assays demonstrate an LD50 value of 13.45 ng/mg and 7.20 ng/mg for the web extract from N. cruentata and T. clavipes, respectively. Overall, these scientific findings represent a valuable repository for further exploration of spider web toxin systems and contribute to elucidating the chemical-ecological role of toxic compounds in the prey capture mechanism of spider webs.