ArticleInfection and immunity2008
Bactericidal antibody responses induced by meningococcal recombinant chimeric factor H-binding protein vaccines.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed, 68 citations in OpenAlex.
- Bactericidal human monoclonal antibody 1B1 shows specificity for meningococcal factor H binding protein variant 2 and displaces human factor H.FASEB bioAdvances · 2024Article
- Insights into structural vaccinology harnessed for universal coronavirus vaccine development.Clinical and experimental vaccine research · 2024Review
- FHbp variants among meningococci of serogroup B in Italy: Evolution and selective pressure, 2014-2017.PloS one · 2023Article
- Structural characterization of a cross-protective natural chimera of factor H binding protein from meningococcal serogroup B strain NL096.Computational and structural biotechnology journal · 2022Article
- Hijacking Factor H for Complement Immune Evasion.Frontiers in immunology · 2021Review
- Molecular characterization of two sub-family specific monoclonal antibodies to meningococcal Factor H binding protein.Heliyon · 2018Article
- The role of apolipoprotein N-acyl transferase, Lnt, in the lipidation of factor H binding protein of Neisseria meningitidis strain MC58 and its potential as a drug target.British journal of pharmacology · 2017Article
- Article
- Meningococcal Factor H Binding Protein Vaccine Antigens with Increased Thermal Stability and Decreased Binding of Human Factor H.Infection and immunity · 2016Article
- A meningococcal vaccine antigen engineered to increase thermal stability and stabilize protective epitopes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Susceptibility of Meningococcal Strains Responsible for Two Serogroup B Outbreaks on U.S. University Campuses to Serum Bactericidal Activity Elicited by the MenB-4C Vaccine.Clinical and vaccine immunology : CVI · 2015Article
- Functional Analysis of the Human Antibody Response to Meningococcal Factor H Binding Protein.mBio · 2015Article
- A Mutant Library Approach to Identify Improved Meningococcal Factor H Binding Protein Vaccine Antigens.PloS one · 2015Article
- A Newly-Identified Polymorphism in Rhesus Macaque Complement Factor H Modulates Binding Affinity for Meningococcal FHbp.PloS one · 2015Article
- Importance of inhibition of binding of complement factor H for serum bactericidal antibody responses to meningococcal factor H-binding protein vaccines.The Journal of infectious diseases · 2013Article
- Defining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigen.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Distinct binding and immunogenic properties of the gonococcal homologue of meningococcal factor h binding protein.PLoS pathogens · 2013Article
- Structural vaccinology starts to deliver.Nature reviews. Microbiology · 2012Review
- Design of meningococcal factor H binding protein mutant vaccines that do not bind human complement factor H.Infection and immunity · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Factor H-binding protein (fHbp) is a novel meningococcal vaccine candidate that elicits serum antibodies that activate classical complement pathway bacteriolysis and also inhibit binding of the complement down-regulatory protein, factor H, to the bacterial surface. One limitation of fHbp as a vaccine candidate is antigenic variability, since antibodies to fHbp in the variant 1 (v.1) antigenic group do not protect against strains expressing v.2 or v.3 proteins, and vice versa. We have identified amino acid residues of epitopes recognized by bactericidal anti-fHbp monoclonal antibodies prepared against fHbp from each of the variant groups. One epitope expressed by nearly all v.1 proteins mapped to the B domain, while epitopes expressed by fHbp v.2 or v.3 mapped to the C domain. The results provided the rationale for engineering chimeric fHbp molecules containing the A domain (which is conserved across all variant groups), a portion of the B domain of a v.1 protein, and the carboxyl-terminal portion of the B domain and the C domain of a v.2 protein. By enzyme-linked immunosorbent assay, the resulting recombinant chimeric proteins expressed epitopes from all three variant groups. In mice, the chimeric vaccines elicited serum antibodies with bactericidal activity against a panel of genetically diverse strains expressing fHbp v.1, v.2, or v.3. The data demonstrate the feasibility of preparing a meningococcal vaccine from a single recombinant protein that elicits broad bactericidal activity, including group B strains, which account for 50 percent of cases of meningococcal disease and for which there currently is no broadly protective vaccine.
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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.