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<p>Arachnids are a specialized class of animals with venom as a biological weapon. Understanding the composition and mode of action is always a fascinating area of research for scientists. Among 53,250 known spider species, the venom of only a few spiders has been characterized thus far. This research contributes to venom isolation using electrostimulation and an understanding of the complex proteome of the small molecular composition of <i>Nephila pilipes</i> (Fabricius, 1793), an Araneidae spider, collected from the Purulia district of West Bengal, India. The electrostimulation method was used for venom extraction from this species. Venom proteins were filtered using 3&#xa0;kDa MWco Amicon filters and then trypsin digested. The proteomic profile was subsequently analyzed using the ESI-nanoLC–MS/MS technique. Eleven protein molecules ranging in mass from 842.0064&#xa0;Da to 48.658&#xa0;kDa were identified. The physicochemical characteristics of the most abundant A0A076KVB0 and A0A076KTH2 venom proteins were analyzed by using bioinformatics. Their functions in terms of hydrolase and peptidase activity, aminoprotease function, lipoic acid metabolism, and the relationships with ABC transporters were revealed via gene ontology enrichment. The presence of domains of unidentified function (DUF4162) indicates possible novel bioactive characteristics of venom proteins. The ESI<sup>+</sup> MS technique was used for understanding venom molecules using low mass profile, and ten acylpolyamines with masses ranging from 330.288&#xa0;Da to 658.439&#xa0;Da were identified. Spider venom proteins and acylpolyamines target ion channels and receptors with precision, showing clues for drug development and therapeutic potential. This pioneering work describes venom isolation and the bioactive components of venom from <i>N. pilipes</i>, and it will inspire spider toxinology research in the Indian as well as global context.</p> Graphical Abstract <p></p>

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Isolation of Nephila pilipes Spider Venom from India by Electrostimulation and Identification of its Proteins and Acylpolyamines by Mass Spectrometry

  • 期刊论文

  • 发表日期：

    2026年1月14日

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  • Mahato Swastik,
  • Ghosh Abhijit,
  • Saha Partha Pratim

摘要

Arachnids are a specialized class of animals with venom as a biological weapon. Understanding the composition and mode of action is always a fascinating area of research for scientists. Among 53,250 known spider species, the venom of only a few spiders has been characterized thus far. This research contributes to venom isolation using electrostimulation and an understanding of the complex proteome of the small molecular composition of Nephila pilipes (Fabricius, 1793), an Araneidae spider, collected from the Purulia district of West Bengal, India. The electrostimulation method was used for venom extraction from this species. Venom proteins were filtered using 3 kDa MWco Amicon filters and then trypsin digested. The proteomic profile was subsequently analyzed using the ESI-nanoLC–MS/MS technique. Eleven protein molecules ranging in mass from 842.0064 Da to 48.658 kDa were identified. The physicochemical characteristics of the most abundant A0A076KVB0 and A0A076KTH2 venom proteins were analyzed by using bioinformatics. Their functions in terms of hydrolase and peptidase activity, aminoprotease function, lipoic acid metabolism, and the relationships with ABC transporters were revealed via gene ontology enrichment. The presence of domains of unidentified function (DUF4162) indicates possible novel bioactive characteristics of venom proteins. The ESI+ MS technique was used for understanding venom molecules using low mass profile, and ten acylpolyamines with masses ranging from 330.288 Da to 658.439 Da were identified. Spider venom proteins and acylpolyamines target ion channels and receptors with precision, showing clues for drug development and therapeutic potential. This pioneering work describes venom isolation and the bioactive components of venom from N. pilipes, and it will inspire spider toxinology research in the Indian as well as global context.

Graphical Abstract