Spider venom has been shown to possess a variety of pharmacological activities with promising applications in biomedical and agricultural sciences. However, the molecular structure and functions of these toxins have only been revealed for a few species. In this study, we unveiled the venom composition of Macrothele washanensis venom for the first time using transcriptomics, proteomics, and bioinformatic analyses. A total of 147,492,716 Illumina valid reads were obtained from the transcriptome of the venom glands, and 3,010,024 unigenes were assembled to predict 69 putative toxin sequences, which were classified into 25 toxin superfamilies based on cysteine motifs. Crude venom proteomics analysis identified 43 toxin proteins, including 15 peptide toxins and 28 proteases, including the CAP (CRISP/Allergen/PR) protein family, acetylcholinesterase, metalloproteinases, hyaluronidase, and dermonecrotic toxin. In conclusion, the results of the present study revealed the composition of the venom of M. washanensis, and several peptide toxins with potential medical, such work provides the foundation for further research on the molecular functions of these venom components as well as applied studies for the use of such compounds.
