ArticlePLoS pathogens2013
Distinct binding and immunogenic properties of the gonococcal homologue of meningococcal factor h binding protein.
Article in PLoS pathogens, 2013. 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.
- Defining the Efficacy of Meningococcal B Vaccines Against Gonococcal Acquisition: The Current Landscape.Journal of the International AIDS Society · 2026Review
- Investigation of Correlates of Protection Against Gonococcal Infection by Comparative Immunoprofiling of Responses in Experimental and Clinical Studies.The Journal of infectious diseases · 2026Article
- Efficacy of the serogroup BBMJ open · 2026Article
- Effectiveness of the four-component protein-based meningococcal vaccine againstCanada communicable disease report = Releve des maladies transmissibles au Canada · 2025Article
- The Neisseria meningitidis Urethritis Clade (NmUC) Acts as a "Chimeric Pathogen" During Infection of Primary, Human Male, Urethral Epithelial Cells.The Journal of infectious diseases · 2025Article
- NHBA antibodies elicited by 4CMenB vaccination are key for serum bactericidal activity against Neisseria gonorrhoeae.NPJ vaccines · 2024Article
- Review
- Article
- PathogenicInfection and immunity · 2022Article
- 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
- 4CMenB Immunization Induces Serum Bactericidal Antibodies Against Non-Serogroup B Meningococcal Strains in Adolescents.Infectious diseases and therapy · 2021Article
- Emergence of a novel urogenital-tropic Neisseria meningitidis.Current opinion in infectious diseases · 2021Review
- Factor H binding protein (fHbp)-mediated differential complement resistance of a serogroup CAccess microbiology · 2021Article
- Hijacking Factor H for Complement Immune Evasion.Frontiers in immunology · 2021Review
- Neisseria meningitidis Urethritis Outbreak Isolates Express a Novel Factor H Binding Protein Variant That Is a Potential Target of Group B-Directed Meningococcal (MenB) Vaccines.Infection and immunity · 2020Article
- The Serogroup B Meningococcal Vaccine Bexsero Elicits Antibodies to Neisseria gonorrhoeae.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2019Article
- Article
- A Meningococcal Native Outer Membrane Vesicle Vaccine With Attenuated Endotoxin and Overexpressed Factor H Binding Protein Elicits Gonococcal Bactericidal Antibodies.The Journal of infectious diseases · 2019Article
- Role of Gonococcal Neisserial Surface Protein A (NspA) in Serum Resistance and Comparison of Its Factor H Binding Properties with Those of Its Meningococcal Counterpart.Infection and immunity · 2019Article
- Progress Toward a Gonococcal Vaccine: The Way Forward.Frontiers in immunology · 2019Review
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
Neisseria meningitidis is a leading cause of sepsis and meningitis. The bacterium recruits factor H (fH), a negative regulator of the complement system, to its surface via fH binding protein (fHbp), providing a mechanism to avoid complement-mediated killing. fHbp is an important antigen that elicits protective immunity against the meningococcus and has been divided into three different variant groups, V1, V2 and V3, or families A and B. However, immunisation with fHbp V1 does not result in cross-protection against V2 and V3 and vice versa. Furthermore, high affinity binding of fH could impair immune responses against fHbp. Here, we investigate a homologue of fHbp in Neisseria gonorrhoeae, designated as Gonococcal homologue of fHbp (Ghfp) which we show is a promising vaccine candidate for N. meningitidis. We demonstrate that Gfhp is not expressed on the surface of the gonococcus and, despite its high level of identity with fHbp, does not bind fH. Substitution of only two amino acids in Ghfp is sufficient to confer fH binding, while the corresponding residues in V3 fHbp are essential for high affinity fH binding. Furthermore, immune responses against Ghfp recognise V1, V2 and V3 fHbps expressed by a range of clinical isolates, and have serum bactericidal activity against N. meningitidis expressing fHbps from all variant groups.
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