Multiomics Profiling of Toxins in the Venom of the Amazonian Spider Acanthoscurria juruenicola

Acanthoscurria juruenicola is an
Amazonian spider described for the first time almost a century ago.
However, little is known about their venom composition. Here, we present
a multiomics characterization of A. juruenicola venom by a combination of transcriptomics, proteomics, and peptidomics
approaches. Transcriptomics of female venom glands resulted in 93,979
unique assembled mRNA transcript encoding proteins. A total of 92
proteins were identified in the venom by mass spectrometry, including
14 mature cysteine-rich peptides (CRPs). Quantitative analysis showed
that CRPs, cysteine-rich secretory proteins, metalloproteases, carbonic
anhydrases, and hyaluronidase comprise >90% of the venom proteome.
Relative quantification of venom toxins was performed by DIA and DDA,
revealing converging profiles of female and male specimens by both
methods. Biochemical assays confirmed the presence of active hyaluronidases,
phospholipases, and proteases in the venom. Moreover, the venom promoted in vivo paralytic activities in crickets, consistent with
the high concentration of CRPs. Overall, we report a comprehensive
analysis of the arsenal of toxins of A. juruenicola and highlight their potential biotechnological and pharmacological
applications. Mass spectrometry data were deposited to the ProteomeXchange
Consortium via the PRIDE repository with the dataset identifier PXD013149
and via the MassIVE repository with the dataset identifier MSV000087777.