ArticleNature communications2020
Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 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.
The trial behind it
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
54 citing papers in PubMed, 91 citations in OpenAlex.
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- Taming Superbugs: Current Progress and Challenges in Combating ESKAPE Pathogens.Pathogens (Basel, Switzerland) · 2025Review
- An LPS-Deficient vaccine candidate with steD deletion confers enhanced protection against homologous and heterologous Salmonella.BMC veterinary research · 2025Article
- Rapid detection and capture of clinical Escherichia coli strains mediated by OmpA-targeting nanobodies.Communications biology · 2025Article
- Proximity biotinylation at the host-bioRxiv : the preprint server for biology · 2025Article
- Genetic engineering of E. coli K-12 for heterologous carbohydrate antigen production.Microbial cell factories · 2025Article
- Evasion of serum antibodies and complement by Salmonella Typhi and Paratyphi A.PLoS pathogens · 2025Article
- Effects of bcsE, luxS and rfaG genes on the physiology and pathogenicity of Salmonella Typhimurium.Archives of microbiology · 2025Article
- Review
- Type 5 secretion system antigens as vaccines against Gram-negative bacterial infections.NPJ vaccines · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
24 authors at 8 institutions in 4 countries.
Funding
Abstract
Lipopolysaccharide (LPS) O-antigen (O-Ag) is known to limit antibody binding to surface antigens, although the relationship between antibody, O-Ag and other outer-membrane antigens is poorly understood. Here we report, immunization with the trimeric porin OmpD from Salmonella Typhimurium (STmOmpD) protects against infection. Atomistic molecular dynamics simulations indicate this is because OmpD trimers generate footprints within the O-Ag layer sufficiently sized for a single IgG Fab to access. While STmOmpD differs from its orthologue in S. Enteritidis (SEn) by a single amino-acid residue, immunization with STmOmpD confers minimal protection to SEn. This is due to the OmpD-O-Ag interplay restricting IgG binding, with the pairing of OmpD with its native O-Ag being essential for optimal protection after immunization. Thus, both the chemical and physical structure of O-Ag are key for the presentation of specific epitopes within proteinaceous surface-antigens. This enhances combinatorial antigenic diversity in Gram-negative bacteria, while reducing associated fitness costs.
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What OpenQuestion holds
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.