Characterization of a new hemolytic protein toxin from the sea anemone Anthopleura asiatica |
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Authors: | Kohno Yuuki Satoh Hiroshi Iguchi Akiko Nagai Hiroshi |
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Institution: | (1) Tokyo University of Marine Science and Technology, 4-5-7 Konan, Minato-ku, Tokyo 108-8477, Japan |
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Abstract: | A 20-kDa protein toxin (bandaporin) was isolated from the sea anemone Anthopleura asiatica (Actiniidae) using the precipitation of ammonium sulfate saturation, and ion-exchange and gel-permeation chromatographies.
Bandaporin showed potent hemolytic activity (EC50 value: 8.8 ng/ml to 0.8% suspension of sheep red blood cells) and lethal toxicity to crayfish (LD100 value: 0.58 mg/kg). The hemolytic activity of bandaporin was inhibited specifically by sphingomyelin. Eight other tested
membrane lipids, including cholesterol, and gangliosides GM1 and GM2, did not inhibit bandaporin hemolytic activity. Antimicrobial
and phospholipase A2 (PLA2) activities were not detected in bandaporin. The complementary DNA (cDNA) encoding bandaporin was sequenced and the deduced
amino acid sequence of bandaporin revealed that this actinoporin had not been previously characterized. Actinoporins are cytolytic
peptide toxins that are widely distributed in Actiniidae and Stichodactylidae sea anemones. This study was the first characterization
of an actinoporin from a sea anemone of the genus Anthopleura. |
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Keywords: | Actinoporin Hemolytic toxin Protein Sea anemone |
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