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Glabralysins, Potential New β-Pore-Forming Toxin Family Members from the Schistosomiasis Vector Snail Biomphalaria glabrata ArchiMer
Lassalle, Damien; Tetreau, Guillaume; Pinaud, Silvain; Galinier, Richard; Crickmore, Neil; Gourbal, Benjamain; Duval, David.
Biomphalaria glabrata is a freshwater Planorbidae snail. In its environment, this mollusk faces numerous microorganisms or pathogens, and has developed sophisticated innate immune mechanisms to survive. The mechanisms of recognition are quite well understood in Biomphalaria glabrata, but immune effectors have been seldom described. In this study, we analyzed a new family of potential immune effectors and characterized five new genes that were named Glabralysins. The five Glabralysin genes showed different genomic structures and the high degree of amino acid identity between the Glabralysins, and the presence of the conserved ETX/MTX2 domain, support the hypothesis that they are pore-forming toxins. In addition, tertiary structure prediction confirms that...
Tipo: Text Palavras-chave: Pore-forming toxin; Cry toxin; Invertebrate; Biomphalaria glabrata; Host; Pathogen; Vector snail; Innate immunity.
Ano: 2020 URL: https://archimer.ifremer.fr/doc/00601/71267/69655.pdf
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Purification of a 19-kDa pore-forming cytolysin from the sea anemone Heteractis magnifica J. Venom. Anim. Toxins incl. Trop. Dis.
Karthikayalu,S; Rama,V; Venkatesan,R.
Pore-forming cytolysins of 19 kDa from sea anemones present a remarkable cytolytic property. In the present work, a purified 19-kDa cytolysin was obtained from the sea anemone Heteractis magnifica. The purification steps involved ammonium sulfate precipitation and subsequently desalting by dialysis against 10 mM sodium phosphate buffer (pH 7.4), followed by anion exchange chromatography in DEAE-Sepharose® column (GE Healthcare, Sweden) and gel filtration chromatography using Sephadex® G-50 matrix (GE Healthcare, Sweden). The active fractions from the gel filtration chromatography were pooled and rechromatographed in the same column. The final active fraction showed a prominent protein band of molecular mass of 19 kDa when analyzed by SDS-PAGE.
Tipo: Info:eu-repo/semantics/other Palavras-chave: Heteractis magnifica; Cytolysin; Hemolysin; Pore-forming toxin.
Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992010000300019
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