77, Sh 28.12 as well as Bg 26.42 (from B. granulifera) exhibited similar chromatographic behavior, molecular masses and effects on crabs, in
relation to sodium channel toxins ShI, BgII and BgIII ( Table 1). Besides the known sodium channel toxins ShI (type 2), BgII, BgIII (type 1) and related fractions Sh 26.77, Sh 28.12 and Bg 26.42 found in the present study, other different sodium channel toxins may be present in chromatographic fractions exhibiting similar effects with lethality to crabs. That is the case of Bg 24.12 and Bg 24.55, which are mainly composed of much smaller peptides (3–3.2 kDa) similarly INCB024360 to type 3 sodium channel toxins Da-I, Da-II, Er-I [36] and PaTX [41]. Another lethal fraction inducing similar effects in comparison with sodium channel toxins
is Bg 21.82, mainly composed of an even smaller peptide (2832 Da). The classification of a toxic peptide ABT-737 of this size as a smaller member of type 3 sodium channel toxins should be confirmed by sequencing. Up to date known sea anemone toxins with molecular masses below 3 kDa remain unclassified. A common feature of the sea anemone species B. granulifera, S. helianthus and B. cangicum [85] is the occurrence of a notable peptide population in the range of 1.5–2 kDa ( Fig. 3D–F), especially abundant in S. helianthus and B. granulifera. Four fractions composed of very small peptides within that molecular mass range exhibited toxicity to crabs: Bg 10.15, Bg 11.52, Bg 11.95 and Bg 12.73 ( Table 1). Up to date no peptide toxin of such small size (at the most 18–19 amino acid residues) has been characterized from sea anemones, therefore these new peptides found in our study are likely to belong to a new class of toxins. In contrast to the above mentioned toxins we have found several fractions that exhibited a very different paralysis pattern from typical effects provoked by sodium channels toxins. Toxic fractions Sh 21.48, Sh 21.61, Bg 19.94, Bg 20.19, Bg 20.79 and Bg Linifanib (ABT-869) 21.57, which are closely related by their similar RPC18 retention times and effects on crabs, also share the presence of
3–4 kDa peptides (being dominant in Sh 21.48 and Sh 21.61). Most of their toxic components seem to be members of the same family, different from sodium channel toxins. Interestingly, a group of toxins with similar chromatographic behavior and molecular masses were isolated from B. cangicum [85] and partially sequenced. Due to the lack of sequence identity with other sea anemone toxins, Bcg 21.00 (3215. 2 Da), Bcg 21.75 (3181 Da) and Bcg 23.41 (3176.4) from B. cangicum were grouped into a novel class of peptides. Other sea anemone toxins with molecular masses in the range of 3–4 kDa comprise some type 1 potassium channel toxins and also several unclassified toxins. However, the fraction (Bg 16.07) identified as BgK (type 1 K+ channel toxin) eluted much earlier than toxins in analysis and had no effect on crabs.
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