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Background <p><i>Sicarius rugosus</i>, the only member of the genus that inhabits Central America, is phylogenetically related to South American <i>Sicarius</i> spiders. These originated from a common ancestor with sister African species. Like <i>Loxosceles</i>, <i>Sicarius</i> exhibits venom phospholipase D activity due to a group of toxins known collectively as SicTox.</p> Methods <p>A gel-assisted, bottom-up, proteomic analysis was performed to characterize the venom composition of <i>S. rugosus</i>. Hyaluronidase activity was determined using zymography.</p> Results <p>We identified several SicTox sequences, all classified as β-clade paralogs and sharing unique peptides with proteins from <i>S. patagonicus</i>, <i>S. peruensis,</i> and other species. Enzymes such as metalloproteinases, including putative astacins, carboxypeptidases, and angiotensin-converting enzymes, were detected in the venom. We also identified probable serine proteinases and a toxin-processing peptidylglycine α-hydroxylating monooxygenase, which may participate in venom peptide maturation. The venom displays in vitro hyaluronidase activity. Some likely peptide toxins were also identified, including a sicaritoxin, which preferentially targets insects.</p> Conclusion <p>This represents the first proteomic study of the rare six-eyed sand spider, <i>S. rugosus</i>, from the dry forest of Costa Rica, confirming the presence of sequences similar to phospholipases D of other <i>Sicarius</i> and <i>Loxosceles</i> species, as well as venom neuropeptides and enzymes characteristic of the family Sicariidae, which may participate in tissue spreading and processing of other venom constituents.</p>

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Venomics of the six-eyed sand spider, Sicarius rugosus (Araneae: Sicariidae), from the neotropical dry forest of Costa Rica

  • 期刊论文

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  • 发表日期：

    2026年4月26日

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  • Cecilia Díaz,
  • Fabián Bonilla,
  • Julián Fernández,
  • Mahmood Sasa

摘要

Background

Sicarius rugosus, the only member of the genus that inhabits Central America, is phylogenetically related to South American Sicarius spiders. These originated from a common ancestor with sister African species. Like Loxosceles, Sicarius exhibits venom phospholipase D activity due to a group of toxins known collectively as SicTox.

Methods

A gel-assisted, bottom-up, proteomic analysis was performed to characterize the venom composition of S. rugosus. Hyaluronidase activity was determined using zymography.

Results

We identified several SicTox sequences, all classified as β-clade paralogs and sharing unique peptides with proteins from S. patagonicus, S. peruensis, and other species. Enzymes such as metalloproteinases, including putative astacins, carboxypeptidases, and angiotensin-converting enzymes, were detected in the venom. We also identified probable serine proteinases and a toxin-processing peptidylglycine α-hydroxylating monooxygenase, which may participate in venom peptide maturation. The venom displays in vitro hyaluronidase activity. Some likely peptide toxins were also identified, including a sicaritoxin, which preferentially targets insects.

Conclusion

This represents the first proteomic study of the rare six-eyed sand spider, S. rugosus, from the dry forest of Costa Rica, confirming the presence of sequences similar to phospholipases D of other Sicarius and Loxosceles species, as well as venom neuropeptides and enzymes characteristic of the family Sicariidae, which may participate in tissue spreading and processing of other venom constituents.