Hidden diversity in plain sight: four new species of Nemesia (Araneae: Mygalomorphae) from the Córdoba Province of Spain

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  Hidden diversity in plain sight: four new species of Nemesia (Araneae: Mygalomorphae) from the Córdoba Province of Spain Abstract A taxonomic revision of the species of Nemesia Audouin, 1826, distributed in the vicinity of Córdoba City, southern Spain, is presented. Four new species are described: Nemesia morana sp. nov. (female), N. kodama sp. nov. (male and female), N. rosae sp. nov. (male and female), and N. tamajoni sp. nov. (male and female). These species are distinguished by distinct morphological characters, including the shape of the spermathecae, palpal bulbs, and spinnerets, as well as by burrow architecture. Fieldwork was conducted across two of the three major habitat types in the region—the humid, forested mountains of Sierra Morena and the croplands and riparian forests of the Guadalquivir Valley—while the third, the “campiña”, which is mainly composed of agricultural landscapes, remains poorly explored. Sampling methods included pitfall trapping and the direct e...

Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities

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Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities

Abstract

Spider venoms are primarily composed of small neurotoxic peptides. However, recent studies suggested a hitherto overlooked diversity of spider venom enzymes, although their functional space still remains largely unexplored. We tested 10 spider venoms for enzymatic activities covering six enzyme classes and found that all tested enzymatic activities can be detected in at least some of the venoms and that hyaluronidases exhibit particularly high enzymatic activities. With this, our study provides functional evidence for the proposed biological significance of enzymes in spider venoms, but more detailed investigations are required.
Dresler, J., Herzig, V., Schulte, L., & Lüddecke, T. (2025). Bioactivity profiling of spider venoms reveals predominant hyaluronidase activities. Toxicon, 108667. https://doi.org/10.1016/j.toxicon.2025.108667