ArticleJournal of molecular biology2014
Glycan specificity of the Vibrio vulnificus hemolysin lectin outlines evolutionary history of membrane targeting by a toxin family.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 53 citations in OpenAlex.
- Uncovering the potential virulence factors of emerging pathogens using AI/ML-based tools: a case study inFrontiers in cellular and infection microbiology · 2025Article
- Genomic Insight into Zoonotic and EnvironmentalMicroorganisms · 2024Article
- Public health aspects ofEFSA journal. European Food Safety Authority · 2024Article
- Investigating diversity and similarity between CBM13 modules and ricin-B lectin domains using sequence similarity networks.BMC genomics · 2024Article
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Genetic and structural basis of the human anti-α-galactosyl antibody response.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.The Journal of membrane biology · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Review
- The role of Vibrio vulnificus virulence factors and regulators in its infection-induced sepsis.Folia microbiologica · 2020Review
- Vibiro vulnificus hemolysin associates with gangliosides.BMC microbiology · 2020Article
- Review
- Functional classification of protein toxins as a basis for bioinformatic screening.Scientific reports · 2017Article
- NMR structure of the Bacillus cereus hemolysin II C-terminal domain reveals a novel fold.Scientific reports · 2017Article
- Article
- Proteomics Analysis Reveals Previously Uncharacterized Virulence Factors in Vibrio proteolyticus.mBio · 2016Article
- Pore-forming toxins: ancient, but never really out of fashion.Nature reviews. Microbiology · 2016Review
- The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin.The Journal of biological chemistry · 2015Article
- Phobalysin, a Small β-Pore-Forming Toxin of Photobacterium damselae subsp. damselae.Infection and immunity · 2015Article
- SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Methods (San Diego, Calif.) · 2015Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Pore-forming toxins (PFTs) are a class of pathogen-secreted molecules that oligomerize to form transmembrane channels in cellular membranes. Determining the mechanism for how PFTs bind membranes is important in understanding their role in disease and for developing possible ways to block their action. Vibrio vulnificus, an aquatic pathogen responsible for severe food poisoning and septicemia in humans, secretes a PFT called V. vulnificus hemolysin (VVH), which contains a single C-terminal targeting domain predicted to resemble a β-trefoil lectin fold. In order to understand the selectivity of the lectin for glycan motifs, we expressed the isolated VVH β-trefoil domain and used glycan-chip screening to identify that VVH displays a preference for terminal galactosyl groups including N-acetyl-d-galactosamine and N-acetyl-d-lactosamine. The X-ray crystal structure of the VVH lectin domain solved to 2.0Å resolution reveals a heptameric ring arrangement similar to the oligomeric form of the related, but inactive, lectin from Vibrio cholerae cytolysin. Structures bound to glycerol, N-acetyl-d-galactosamine, and N-acetyl-d-lactosamine outline a common and versatile mode of recognition allowing VVH to target a wide variety of cell-surface ligands. Sequence analysis in light of our structural and functional data suggests that VVH may represent an earlier step in the evolution of Vibrio PFTs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.