ArticleHybridoma (2005)2011
Characterization of monoclonal antibodies to terminal and internal O-antigen epitopes of Francisella tularensis lipopolysaccharide.
Article in Hybridoma (2005), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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Who cites it
19 citing papers in PubMed, 25 citations in OpenAlex.
- Comparison of O-specific polysaccharide responses in patients following infection withmSphere · 2023Article
- Article
- Article
- Inhibition of Francisella tularensis phagocytosis using a novel anti-LPS scFv antibody fragment.Scientific reports · 2019Article
- Aerosol prime-boost vaccination provides strong protection in outbred rabbits against virulent type A Francisella tularensis.PloS one · 2018Article
- Immunoglobulin G subclass switching impacts sensitivity of an immunoassay targeting Francisella tularensis lipopolysaccharide.PloS one · 2018Article
- An O-Antigen Glycoconjugate Vaccine Produced Using Protein Glycan Coupling Technology Is Protective in an Inhalational Rat Model of Tularemia.Journal of immunology research · 2018Article
- A semisyntheticScience translational medicine · 2017Article
- Technologies for Proteome-Wide Discovery of Extracellular Host-Pathogen Interactions.Journal of immunology research · 2017Review
- Article
- Functional and structural characterization of Francisella tularensis O-antigen antibodies at the low end of antigen reactivity.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2014Article
- Discovery of protective B-cell epitopes for development of antimicrobial vaccines and antibody therapeutics.Immunology · 2014Review
- Antibodies to both terminal and internal B-cell epitopes of Francisella tularensis O-polysaccharide produced by patients with tularemia.Clinical and vaccine immunology : CVI · 2014Article
- B-cell epitopes in GroEL of Francisella tularensis.PloS one · 2014Article
- Metabolic labeling to characterize the overall composition of Francisella lipid A and LPS grown in broth and in human phagocytes.Innate immunity · 2014Article
- The binding sites of monoclonal antibodies to the non-reducing end of Francisella tularensis O-antigen accommodate mainly the terminal saccharide.Immunology · 2013Article
- Structural analysis of a protective epitope of the Francisella tularensis O-polysaccharide.Biochemistry · 2012Article
- Protective B-cell epitopes of Francisella tularensis O-polysaccharide in a mouse model of respiratory tularaemia.Immunology · 2012Article
- A typical preparation of Francisella tularensis O-antigen yields a mixture of three types of saccharides.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The lipopolysaccharide (LPS) of Francisella tularensis (Ft), the Gram negative bacterium that causes tularemia, has been shown to be a main protective antigen in mice and humans; we have previously demonstrated that murine anti-Ft LPS IgG2a monoclonal antibodies (MAbs) can protect mice against otherwise lethal intranasal infection with the Ft live vaccine strain (LVS). Here we show that four IgG2a anti-LPS MAbs are specific for the O-polysaccharide (O-antigen [OAg]) of Ft LPS. But whereas three of the MAbs bind to immunodominant repeating internal epitopes, one binds to a unique terminal epitope of Ft OAg. This was deduced from its even binding to both long and short chains of the LPS ladder in Western blots, its rapid decrease in ELISA binding to decreasing solid-phase LPS concentrations, its inability to compete for LPS binding with a representative of the other three MAbs, and its inability to immunoprecipitate OAg despite its superior agglutination titer. Biacore analysis showed the end-binding MAb to have higher bivalent avidity for Ft OAg than the internal-binding MAbs and provided an immunogenicity explanation for the predominance of internal-binding anti-Ft OAg MAbs. These findings demonstrate that non-overlapping epitopes can be targeted by antibodies to Ft OAg, which may inform the design of vaccines and immunotherapies against tularemia.
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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.