Transcriptome and proteomic analysis reveals a diverse range of venoms in the recently described spider species Macrothele Washanensis

Spider Venom has been shown to have a variety of pharmacological activities with promising applications in biomedical and agricultural sciences. However, the molecular structure and function of these toxins have been revealed only for a small number of species. This study published the composition of venom Macrothele Washanensis First time using venom, proteomics, and bioinformatic analysis. A total of 147,492,716 Illumina valid reads were obtained from the transcriptome of the venom gland, and 3,010,024 unigens were assembled, predicting 69 putative toxin sequences. Crude toxin proteomics analysis identified 43 toxin proteins, including 15 peptide toxins, including CAP (crisp/allergen/PR) protein family, acetylcholinesterase, metalloproteinase, hyaluronidase, and toxins that bind to delmon, and 43 toxin proteins. In conclusion, the results of this study are M. Washanensisand some peptide toxins that have received potential medical care provide such research, the basis for further research into the molecular function of these venom components, and applied studies on the use of such compounds.