Biomphalysin, a New β Pore-forming Toxin Involved in Biomphalaria glabrata Immune Defense against Schistosoma mansoni
Richard Galinier,Julien Portela,Julien Portela,Yves Moné,Yves Moné,Yves Moné,Jean-François Allienne,Jean-François Allienne,Hélène Henri,Stephane Delbecq,Guillaume Mitta,Guillaume Mitta,Benjamin Gourbal,Benjamin Gourbal,David Duval,David Duval +15 more
TLDR
These results provide the first functional description of a mollusk immune effector protein involved in killing S. mansoni and show that, in contrast to what has been reported for most other members of the family, lytic activity of Biomphalysin is not dependent on proteolytic processing.Abstract:
Aerolysins are virulence factors belonging to the β pore-forming toxin (β-PFT) superfamily that are abundantly distributed in bacteria. More rarely, β-PFTs have been described in eukaryotic organisms. Recently, we identified a putative cytolytic protein in the snail, Biomphalaria glabrata, whose primary structural features suggest that it could belong to this β-PFT superfamily. In the present paper, we report the molecular cloning and functional characterization of this protein, which we call Biomphalysin, and demonstrate that it is indeed a new eukaryotic β-PFT. We show that, despite weak sequence similarities with aerolysins, Biomphalysin shares a common architecture with proteins belonging to this superfamily. A phylogenetic approach revealed that the gene encoding Biomphalysin could have resulted from horizontal transfer. Its expression is restricted to immune-competent cells and is not induced by parasite challenge. Recombinant Biomphalysin showed hemolytic activity that was greatly enhanced by the plasma compartment of B. glabrata. We further demonstrated that Biomphalysin with plasma is highly toxic toward Schistosoma mansoni sporocysts. Using in vitro binding assays in conjunction with Western blot and immunocytochemistry analyses, we also showed that Biomphalysin binds to parasite membranes. Finally, we showed that, in contrast to what has been reported for most other members of the family, lytic activity of Biomphalysin is not dependent on proteolytic processing. These results provide the first functional description of a mollusk immune effector protein involved in killing S. mansoni.read more
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Journal ArticleDOI
Pore-forming toxins: ancient, but never really out of fashion
TL;DR: The diverse pore architectures and membrane insertion mechanisms that have been revealed by structural studies of PFTs are discussed, and how these features contribute to binding specificity for different membrane targets are considered.
Journal ArticleDOI
Why do we study animal toxins
TL;DR: The mission is to find out the right natural pairings and interactions of the authors' body elements with toxins, and with endogenous toxin-like molecules, and to propose the natural pairing hypothesis, which links toxins with humans.
Journal ArticleDOI
Advances in gastropod immunity from the study of the interaction between the snail Biomphalaria glabrata and its parasites: A review of research progress over the last decade
Christine Coustau,Benjamin Gourbal,David Duval,Timothy P. Yoshino,Coen M. Adema,Guillaume Mitta +5 more
TL;DR: The current overview emphasizes that the interaction between B. glabrata and its trematode parasites involves a complex molecular crosstalk between numerous antigens, immune receptors, effectors and anti-effector systems that are highly diverse structurally and extremely variable in expression between and within host and parasite populations.
Journal ArticleDOI
A Shift from Cellular to Humoral Responses Contributes to Innate Immune Memory in the Vector Snail Biomphalaria glabrata
Silvain Pinaud,Julien Portela,David Duval,Fanny Nowacki,Fanny Nowacki,Marie-Aude Olive,Jean-François Allienne,Richard Galinier,Nolwenn M. Dheilly,Nolwenn M. Dheilly,Sylvie Kieffer-Jaquinod,Guillaume Mitta,André Théron,Benjamin Gourbal +13 more
TL;DR: The first evidence that a shift from a cellular immune response to a humoral immune response occurs during the development of innate memory is provided, in the Lophotrochozoan snail, Biomphalaria glabrata.
ComponentDOI
Clostridium perfringens epsilon toxin shows structural similarity with the pore forming toxin aerolysin
TL;DR: The crystal structure of epsilon-toxin is reported, which reveals structural similarity to aerolysin from Aeromonas hydrophila, which can change conformation between soluble and transmembrane states.
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