ArticleInfection and immunity2003
The C-terminal domain of Salmonella enterica serovar typhimurium OmpA is an immunodominant antigen in mice but appears to be only partially exposed on the bacterial cell surface.
Article in Infection and immunity, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 67 citations in OpenAlex.
- NlpE Is an OmpA-Associated Outer Membrane Sensor of the Cpx Envelope Stress Response.Journal of bacteriology · 2023Article
- Immunoaffinity-based mass spectrometric characterization of immunoreactive proteins ofSaudi journal of biological sciences · 2023Article
- Extracellular vesicles elicit protective immune responses against Salmonella infection.Journal of extracellular vesicles · 2022Article
- Interaction of Liberibacter Solanacearum with Host Psyllid Vitellogenin and Its Association with Autophagy.Microbiology spectrum · 2022Article
- Insight into the Structure, Functions, and Dynamics of theMembranes · 2022Review
- The role of TolA, TolB, and TolR in cell morphology, OMVs production, and virulence of Salmonella Choleraesuis.AMB Express · 2022Article
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- Antigen-encapsulating host extracellular vesicles derived from Salmonella-infected cells stimulate pathogen-specific Th1-type responses in vivo.PLoS pathogens · 2021Article
- Article
- Outer membrane protein size and LPS O-antigen define protective antibody targeting to the Salmonella surface.Nature communications · 2020Article
- Comparison of Humoral Immune Responses to Different Forms ofFrontiers in veterinary science · 2020Article
- Article
- Escherichia coli outer membrane protein F (OmpF): an immunogenic protein induces cross-reactive antibodies against Escherichia coli and Shigella.AMB Express · 2017Article
- Insights into PG-binding, conformational change, and dimerization of the OmpA C-terminal domains from Salmonella enterica serovar Typhimurium and Borrelia burgdorferi.Protein science : a publication of the Protein Society · 2017Article
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- Recombinant Salmonella typhimurium outer membrane protein A is recognized by synovial fluid CD8 cells and stimulates synovial fluid mononuclear cells to produce interleukin (IL)-17/IL-23 in patients with reactive arthritis and undifferentiated spondyloarthropathy.Clinical and experimental immunology · 2016Article
- Protective efficacy by various doses of Salmonella ghost vaccine candidate carrying enterotoxigenic Escherichia coli fimbrial antigen against neonatal piglet colibacillosis.Canadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2016Article
- Immunogenicity and Cross-Protective Efficacy Induced by Outer Membrane Proteins from Salmonella Typhimurium Mutants with Truncated LPS in Mice.International journal of molecular sciences · 2016Article
- Serotype O18 avian pathogenic and neonatal meningitis Escherichia coli strains employ similar pathogenic strategies for the onset of meningitis.Virulence · 2015Article
- Salmonella enterica serovar enteritidis ghosts carrying the Escherichia coli heat-labile enterotoxin B subunit are capable of inducing enhanced protective immune responses.Clinical and vaccine immunology : CVI · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
We examined the way the major outer membrane protein OmpA of Salmonella enterica serovar Typhimurium is recognized by the mouse immune system, by raising a panel of 12 monoclonal antibodies (MAbs) against this protein. Interaction between OmpA and these MAbs is competitively inhibited with several-hundredfold dilutions of mouse polyclonal sera obtained by immunization with live or heat-killed whole cells, suggesting that OmpA is one of the immunodominant antigens of serovar Typhimurium. All of the MAbs were specific for an identical epitope(s) located on the C-terminal domain of OmpA, as indicated by the use of OmpA fragments generated by protease or cyanogen bromide treatment and by competitive inhibition enzyme-linked immunosorbent assay. This epitope was highly conserved within (but not outside) the family Enterobacteriaceae: The strong immunogenicity of this epitope was surprising because the C-terminal domain of OmpA, usually thought to be located in the periplasm, is not expected to be exposed on the bacterial cell surface. A MAb, however, reacted in a cytofluorometry assay more strongly with outer-membrane-permeabilized cells than with untreated cells, a result supporting the predominantly periplasmic localization of the epitope. Significant, though low-level, reactivity of intact cells nevertheless suggests that in some cells the C-terminal domain of OmpA is exposed on the surface, a result consistent with the proposal that OmpA can fold into one of the two alternate conformations.
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