ArticleThe Journal of biological chemistry2013
Molecular architecture and functional analysis of NetB, a pore-forming toxin from Clostridium perfringens.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
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Who cites it
53 citing papers in PubMed, 106 citations in OpenAlex.
- Innovative Approaches Against Planktonic and Biofilm-ProducingVeterinary sciences · 2026Review
- Identification and structural characterization of anthrax toxin receptor 2 as the Clostridium perfringens NetF receptor.Nature communications · 2026Article
- Milestones in Clostridium perfringens research since 1995.Anaerobe · 2025Review
- Eimeria: Navigating complex intestinal ecosystems.PLoS pathogens · 2024Review
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Overview of Bacterial Protein Toxins from Pathogenic Bacteria: Mode of Action and Insights into Evolution.Toxins · 2024Review
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
- Structural journey of an insecticidal protein against western corn rootworm.Nature communications · 2023Article
- Evaluation of gene expression related to immunity, apoptosis, and gut integrity that underlies3 Biotech · 2023Article
- Cryo-EM structure of the octameric pore of Clostridium perfringens β-toxin.EMBO reports · 2022Article
- Lactobacillus casei displaying Clostridium perfringens NetB antigen protects chickens against necrotic enteritis.Applied microbiology and biotechnology · 2022Article
- Recombinant Limosilactobacillus (Lactobacillus) delivering nanobodies against Clostridium perfringens NetB and alpha toxin confers potential protection from necrotic enteritis.MicrobiologyOpen · 2022Article
- Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Article
- Toxigenic Profile ofComparative medicine · 2022Article
- PglB function and glycosylation efficiency is temperature dependent when the pgl locus is integrated in the Escherichia coli chromosome.Microbial cell factories · 2022Article
- Role ofVaccines · 2021Review
- Pathogenicity and virulence ofVirulence · 2021Article
- Multivalent poultry vaccine development using Protein Glycan Coupling Technology.Microbial cell factories · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
NetB is a pore-forming toxin produced by Clostridium perfringens and has been reported to play a major role in the pathogenesis of avian necrotic enteritis, a disease that has emerged due to the removal of antibiotics in animal feedstuffs. Here we present the crystal structure of the pore form of NetB solved to 3.9 Å. The heptameric assembly shares structural homology to the staphylococcal α-hemolysin. However, the rim domain, a region that is thought to interact with the target cell membrane, shows sequence and structural divergence leading to the alteration of a phosphocholine binding pocket found in the staphylococcal toxins. Consistent with the structure we show that NetB does not bind phosphocholine efficiently but instead interacts directly with cholesterol leading to enhanced oligomerization and pore formation. Finally we have identified conserved and non-conserved amino acid positions within the rim loops that significantly affect binding and toxicity of NetB. These findings present new insights into the mode of action of these pore-forming toxins, enabling the design of more effective control measures against necrotic enteritis and providing potential new tools to the field of bionanotechnology.
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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.