K. Shiomi et al., NOVEL POLYPEPTIDE TOXINS WITH CRAB LETHALITY FROM THE SEA-ANEMONE ANEMONIA-ERYTHRAEA, Biochimica et biophysica acta (G). General subjects, 1335(1-2), 1997, pp. 191-198
The sea anemone Anernonia erythraea was found to contain polypeptide t
oxins with crab lethality as well as hemolysins. Three polypeptide tox
ins (AETX I, II and III) were isolated by gel filtration on Sephadex G
-50 and reverse-phase HPLC on TSKgel ODS-120T. A geographic variation
in toxin composition was suggested. The LD50 against crabs of AETX I,
II and III were estimated to be 2.2, 0.53 and 0.28 mu g/kg, respective
ly, but none of the toxins showed lethality in mice. The amino acid se
quences of the three toxins were deduced from sequencings of the whole
molecules and their enzymatic fragments. Amino acid analyses and mole
cular mass determinations supported the accuracy of the deduced sequen
ces. AETX I, comprising 47 amino acid residues including 6 half-Cys re
sidues, is an analog of sea anemone type 1 toxins. On the other hand,
AETX II and III, which are highly homologous with each other, are quit
e distinct from the known sea anemone polypeptide toxins in that they
are composed of 59 residues including 10 half-Cys residues. Interestin
gly, both toxins have sequence similarities with neurotoxins isolated
from the Brazilian 'armed' spider Phoneutria nigriventer.