ArticleEMBO reports2016
Structural basis for receptor recognition and pore formation of a zebrafish aerolysin-like protein.
Article in EMBO reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 81 citations in OpenAlex.
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- Natterin bridges IFN-φ1 and non-canonical inflammasome pathways viaFrontiers in cellular and infection microbiology · 2025Article
- Phylogeny, envenomation syndrome, and membrane permeabilising venom produced by Australia's electric caterpillar Comana monomorpha.Scientific reports · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Article
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- Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals.Cells · 2023Review
- Effective Pre-Clinical Treatment of Fish Envenoming with Polyclonal Antiserum.International journal of molecular sciences · 2023Article
- Evaluation of Proteomic and Lipidomic Changes inInternational journal of molecular sciences · 2022Article
- The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3.Communications biology · 2022Article
- Lamprey immune protein triggers the ferroptosis pathway during zebrafish embryonic development.Cell communication and signaling : CCS · 2022Article
- An Update of Lectins from Marine Organisms: Characterization, Extraction Methodology, and Potential Biofunctional Applications.Marine drugs · 2022Review
- Natterin-like depletion by CRISPR/Cas9 impairs zebrafish (Danio rerio) embryonic development.BMC genomics · 2022Article
- First Insights into the Repertoire of Secretory Lectins in Rotifers.Marine drugs · 2022Article
- MicroRNA expression profile in Lampetra morii upon Vibrio anguillarum infection and miR-4561 characterization targeting lip.Communications biology · 2021Article
- The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function.Toxins · 2021Review
- Animal secretory endolysosome channel discovery.Zoological research · 2021Review
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Authors and funding
19 authors at 7 institutions in 2 countries.
Funding
Abstract
Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the lectin module toward high-mannose glycans triggers drastic conformational changes of the aerolysin module in a pH-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.
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