PROTEO-TRANSCRIPTOMIC ANALYSIS IDENTIFIES POTENTIAL NOVEL TOXINS SECRETED BY THE PREDATORY, PREY-PIERCING RIBBON WORM AMPHIPORUS LACTIFLOREUS

Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus

Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus

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Nemerteans (ribbon worms) employ toxins to subdue their prey, but research thus far has focused on the small-molecule components of mucus secretions and few protein toxins have been characterized.We carried out a preliminary proteotranscriptomic analysis of putative toxins produced by the hoplonemertean Amphiporus lactifloreus (Hoplonemertea, Amphiporidae).No variants were found of known opi the color that keeps on giving nemertean-specific toxin proteins (neurotoxins, cytotoxins, parbolysins or nemertides) but several toxin-like transcripts were discovered, expressed strongly in the proboscis, including putative metalloproteinases and sequences resembling sea anemone actitoxins, crown-of-thorn sea star plancitoxins, and multiple classes of inhibitor cystine knot/knottin family proteins.Some of these products were also directly identified in the mucus proteome, supporting their preliminary identification as secreted toxin components.

Two new swish supreme glide track white nemertean-typical toxin candidates could be described and were named U-nemertotoxin-1 and U-nemertotoxin-2.Our findings provide insight into the largely overlooked venom system of nemerteans and support a hypothesis in which the nemertean proboscis evolved in several steps from a flesh-melting organ in scavenging nemerteans to a flesh-melting and toxin-secreting venom apparatus in hunting hoplonemerteans.

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