ArticlePLoS pathogens2013
Biomphalysin, a new β pore-forming toxin involved in Biomphalaria glabrata immune defense against Schistosoma mansoni.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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63 citing papers in PubMed.
- Epigenetic and metabolic reprogramming of innate immune cells establishes immunological memory in the Schistosomiasis vector snail Biomphalaria glabrata.PLoS pathogens · 2026Article
- A systems-level analysis of global gene expression in resistant and susceptibleFrontiers in immunology · 2026Article
- Schistosome exposure and diet induced effects on candidate immune gene expression in an African snail vector.Journal of helminthology · 2025Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- The structural features and immunological role of biomphalysins in the snail Biomphalaria glabrata.PLoS pathogens · 2025Article
- Probing Bacterial Interactions with theToxins · 2025Article
- Schistosome exposure and diet induced effects on candidate immune gene expression in an African snail vector.bioRxiv : the preprint server for biology · 2025Article
- Multiple Horizontal Transfers of Immune Genes Between Distantly Related Teleost Fishes.Molecular biology and evolution · 2025Article
- Genomic basis of schistosome resistance in a molluscan vector of human schistosomiasis.iScience · 2025Article
- Unveiling the hemolymphatic miRNome composition of the schistosomiasis vector snailCurrent research in parasitology & vector-borne diseases · 2025Article
- Comparative immunological roles of TEP1 inFrontiers in immunology · 2025Review
- Exploring the genome-wide transcriptomic responses of Bulinus truncatus to Schistosoma haematobium infection: An important host-parasite system involved in the transmission of human urogenital schistosomiasis.Molecular immunology · 2024Article
- Lipids from a snail host regulate the multicellular behavior of a predator of parasitic schistosomes.iScience · 2024Article
- Host lipids regulate multicellular behavior of a predator of a human pathogen.bioRxiv : the preprint server for biology · 2024Article
- Exploring the immune interactions between Oncomelania hupensis and Schistosoma japonicum, with a cross-comparison of immunological research progress in other intermediate host snails.Parasites & vectors · 2023Review
- Status Quo and Future Perspectives of Molecular and Genomic Studies on the GenusInternational journal of molecular sciences · 2023Review
- A genome sequence for Biomphalaria pfeifferi, the major vector snail for the human-infecting parasite Schistosoma mansoni.PLoS neglected tropical diseases · 2023Article
- Enhanced Hemolytic Activity of MesophilicMicroorganisms · 2022Article
- The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3.Communications biology · 2022Article
- Compatibility between snails and schistosomes: insights from new genetic resources, comparative genomics, and genetic mapping.Communications biology · 2022Article
3 more citing papers are in PubMed but not listed here.
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9 authors.
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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.
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