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A large fraction of the proteins secreted by prawns may be of bacterial origin. We recently isolated a large number of PCR-amplified peptides from the hemocyte cDNA of the prawn Marsupium semisulcatus that were of unknown identity and displayed sequence similarity with components of scorpion toxin-like cysteine-rich venom peptides from the American Brown Recluse spider (Loxosceles reclusa) and African Black Widow spider (Latrodectus tredecimguttatus). Upon alignment analysis, a portion of the same peptides showed strong similarities to the cysteine-rich secretory proteins of the same spiders. Therefore, we hypothesize that these proteins could be composed of a cysteine-rich variable domain flanked by two invariable repeats. We provide an in silico identification of the two types of sequences (minimal repeats and cysteine-rich variable domain) and propose the coding sequence of a novel type of peptide, the penaeidins, in the shrimp. The penaeidins are synthesized by the hepatopancreas and stored in the adductor muscle. Using the database search with a reverse algorithm, we identified a large number of sequences showing similarity to the penaeidins, and, after clustering, we selected the penaeidin variants for further analysis. Since the structure of the penaeidin proteins does not follow any of the known structural models for previously characterized scorpion toxins, they are probably of a new structural class and we propose the name of penaeidins for them.Brass Fly
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