yessotoxin and Hemolysis

Ladder-shaped polyether compounds, represented by brevetoxins, ciguatoxins, maitotoxin, and prymnesins, are thought to possess the high affinity to transmembrane proteins. As a model compound of ladder-shaped polyethers, we adopted desulfated yessotoxin (2) and examined its interaction with glycopholin A, a membrane protein known to form a dimer or oligomer. Desulfated yessotoxin turned out to interact with the alpha-helix so as to induce the dissociation of glycopholin oligomers when examined by SDS and PFO gel electrophoresis. The results provided the first evidence that ladder-shaped polyethers interact with transmembrane helix domains.

Topics: Amino Acid Sequence; Electrophoresis, Polyacrylamide Gel; Ethers, Cyclic; Glycophorins; Hemolysis; Membrane Proteins; Molecular Sequence Data; Mollusk Venoms; Oxocins; Peptides

Yessotoxin (YTX), originally found in association with diarrhetic shellfish poisoning (DSP), caused neither intestinal fluid accumulation nor inhibition of protein phosphatase 2A. Orally, YTX was not lethal to mice at 1.0 mg/kg. The toxin showed weak cytotoxic and antifungal activities. Neither hemolytic nor ichthyotoxic effect was observed.

Topics: Animals; Animals, Suckling; Anti-Infective Agents; Cell Survival; Diarrhea; Dose-Response Relationship, Drug; Enzyme Inhibitors; Ethers, Cyclic; Hemolysis; Male; Mice; Mollusk Venoms; Oxocins; Phosphoprotein Phosphatases; Protein Phosphatase 2; Zebrafish