Molecular cloning and functional expression of hemolysin from the sea anemone Actineria villosa

The equinatoxin N‐terminus is transferred across planar lipid membranes and helps to stabilize the transmembrane pore

“…An arrow denotes the thrombin cleavage site. (D) The alignment of known N-terminal sequences of actinoporins compiled from the literature [8,[45][46][47][48][49]. Hydrophobic amino acids (AGVLIFWYP) are shown in black, polar amino acids (TSMCNQ) are shown in dark gray, and charged amino acids (DEKHR) are shown in light gray.…”

The multigene families of actinoporins (part I): Isoforms and genetic structure

“…The first intron with identical length (242 bp) for both Avts isoforms was found within the 50-untranslated region, and the second intron with length of 654 bp Anderluh et al, 1999), II (EqtII, Anderluh et al, 1996) from Actinia equine, Bandaporin-I (BnpI, Kohno et al, 2009) from Anthopleura asi atica, SrcI (Jiang et al, 2003) from Sagartia rosea, UrcI (Razpotnik et al, 2009) from Urticina crassicornis, H. magnificalysin III (HMgIII, Wang et al, 2000) from Heteractis magnifica, gigantoxin IV (GigtIV, Hu et al, 2011) from Stichodactyla gigantea, PsTX-20A (Nagai et al, 2002) from Phyllodiscus semoni, Avts I and II (Uechi et al, 2005(Uechi et al, , 2010 from Actineria villosa and StII (CIV) from Stichodactyla helianthus. The sequences were aligned with the NTI Vector 9.0.0 program (Informax Inc, EUA) (Henikoff and Henikoff, 1992).…”

Marine Protein Toxins

“…Thus, the mode of action of these MACPF toxins may be explained by their pore-forming activity, in a manner similar to the way in which MACPF proteins function in the mammalian immune system. Actinoporins PsTX-20A [63] and Avt-I [64] have also been isolated as minor toxic components from the nematocyst venom of P. semoni and A. villosa, respectively. On rare occasions, a sting by P. semoni may cause acute renal failure in humans [65].…”