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The Proteotranscriptomic Characterization of Venom in the White Seafan Elucidates the Evolution of Octocorallia Arsenal

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Journal Open Biol
Date 2025 Mar 11
PMID 40068811
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Abstract

All the members of the phylum Cnidaria are characterized by the production of venom in specialized structures, the nematocysts. Venom of jellyfish (Medusozoa) and sea anemones (Anthozoa) has been investigated since the 1970s, revealing a remarkable molecular diversity. Specifically, sea anemones harbour a rich repertoire of neurotoxic peptides, some of which have been developed in drug leads. However, venoms of the vast majority of Anthozoa species remain uncharacterized, particularly in the class Octocorallia. To fill this gap, we applied a proteo-transcriptomic approach to investigate venom composition in , a gorgonian species common in Mediterranean hard-bottom benthic communities. Our results highlighted the peculiarities of the venom of with respect to sea anemones, which is reflected in the presence of several toxins with novel folds, worthy of functional characterization. A comparative genomic survey across the octocoral radiation allowed us to generalize these findings and provided insights into the evolutionary history, molecular diversification patterns and putative adaptive roles of venom toxins. A comparison of whole-body and nematocyst proteomes revealed the presence of different cytolytic toxins inside and outside the nematocysts. Two instances of differential maturation patterns of toxin precursors were also identified, highlighting the intricate regulatory pathways underlying toxin expression.

Citing Articles

The proteotranscriptomic characterization of venom in the white seafan elucidates the evolution of Octocorallia arsenal.

Modica M, Leone S, Gerdol M, Greco S, Aurelle D, Oliverio M Open Biol. 2025; 15(3):250015.

PMID: 40068811 PMC: 11896702. DOI: 10.1098/rsob.250015.

References
1.
Madio B, King G, Undheim E . Sea Anemone Toxins: A Structural Overview. Mar Drugs. 2019; 17(6). PMC: 6627431. DOI: 10.3390/md17060325. View

2.
Kaser A, Winklmayr M, Lepperdinger G, Kreil G . The AVIT protein family. Secreted cysteine-rich vertebrate proteins with diverse functions. EMBO Rep. 2003; 4(5):469-73. PMC: 1319185. DOI: 10.1038/sj.embor.embor830. View

3.
Kozlov S, Grishin E . The universal algorithm of maturation for secretory and excretory protein precursors. Toxicon. 2007; 49(5):721-6. DOI: 10.1016/j.toxicon.2006.11.007. View

4.
Garcia-Fernandez R, Peigneur S, Pons T, Alvarez C, Gonzalez L, Chavez M . The Kunitz-Type Protein ShPI-1 Inhibits Serine Proteases and Voltage-Gated Potassium Channels. Toxins (Basel). 2016; 8(4):110. PMC: 4848636. DOI: 10.3390/toxins8040110. View

5.
Modica M, Lombardo F, Franchini P, Oliverio M . The venomous cocktail of the vampire snail Colubraria reticulata (Mollusca, Gastropoda). BMC Genomics. 2015; 16:441. PMC: 4460706. DOI: 10.1186/s12864-015-1648-4. View