New predatory interaction of Trichonephila clavipes (Araneae: Nephilidae) on Fidicinini (Hemiptera: Cicadidae) in a forest fragment of the Neotropical region

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  New predatory interaction of Trichonephila clavipes (Araneae: Nephilidae) on Fidicinini (Hemiptera: Cicadidae) in a forest fragment of the Neotropical region Abstract Trichonephila clavipes (Araneae: Nephilidae) is an orb web-building spider whose diet is primarily based on flying insects. This note aims to report the first predatory interaction of T. clavipes on a cicada of the genus Fidicina (Hemiptera: Cicadidae) in a fragment of the Atlantic Forest in Brazil. The predation event was observed (ad libitum) in the Benjamin Maranhão Botanical Garden situated in the Mata do Buraquinho Wildlife Refuge, northeastern Brazil. A specimen of Fidicina sp. was found freshly dead and trapped in the web of T. clavipes. The nephilid was observed moving slowly between the ventral and dorsal regions of the Fidicina sp. without weaving a web around the cicadid. Then, T. clavipes was observed perched on the left side of the Fidicina sp., with its pedipalps and chelicerae manipulating the thorax ...

Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species

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Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species

Abstract

The Brazilian scorpion Tityus melici, native to Minas Gerais and Bahia, is morphologically related to Tityus serrulatus, the most medically significant species in Brazil. Despite inhabiting scorpion-envenomation endemic regions, T. melici venom remains unexplored. This work evaluates T. melici venom composition and function using transcriptomics, enzymatic activities, and in vivo and in vitro immunological analyses. Next-Generation Sequencing unveiled 86 components putatively involved in venom toxicity: 39 toxins, 28 metalloproteases, seven disulfide isomerases, six hyaluronidases, three phospholipases and three amidating enzymes. T. serrulatus showed the highest number of toxin matches with 80–100 % sequence similarity. T. melici is of medical importance as it has a venom LD50 of 0.85 mg/kg in mice. We demonstrated venom phospholipase A2 activity, and elevated hyaluronidase and metalloprotease activities compared to T. serrulatus, paralleling our transcriptomic findings. Comparison of transcriptional levels for T. serrulatus and T. melici venom metalloenzymes suggests species-specific expression patterns in Tityus. Despite close phylogenetic association with T. serrulatus inferred from COI sequences and toxin similarities, partial neutralization of T. melici venom toxicity was achieved when using the anti-T. serrulatus antivenom, implying antigenic divergence among their toxins. We suggest that the Brazilian therapeutic scorpion antivenom could be improved to effectively neutralize T. melici venom.


Kalapothakis, Y., Miranda, K., Aragão, M., Larangote, D., Braga-Pereira, G., Noetzold, M., Molina, D., Langer, R., Conceição, I. M., Guerra-Duarte, C., Chávez-Olórtegui, C., Kalapothakis, E., & Borges, A. (2024). Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species. International Journal of Biological Macromolecules, 130311. https://doi.org/10.1016/j.ijbiomac.2024.130311