ArticleInfection and immunity2004
Vaccine potential of the Neisseria meningitidis 2086 lipoprotein.
Article in Infection and immunity, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 166 papers.
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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
166 citing papers in PubMed, 333 citations in OpenAlex.
- Meningococcal Serogroup B Bivalent rLP2086 Vaccine Elicits Broad and Robust Serum Bactericidal Responses in Healthy Adolescents.Journal of the Pediatric Infectious Diseases Society · 2016Trial
- Immunogenicity, Safety, and Tolerability of Bivalent rLP2086 Meningococcal Group B Vaccine Administered Concomitantly With Diphtheria, Tetanus, and Acellular Pertussis and Inactivated Poliomyelitis Vaccines to Healthy Adolescents.Journal of the Pediatric Infectious Diseases Society · 2016Trial
- Phase I safety and immunogenicity study of a candidate meningococcal disease vaccine based on Neisseria lactamica outer membrane vesicles.Clinical and vaccine immunology : CVI · 2009Trial
- Interlaboratory study to assess precision and reproducibility of the meningococcal antigen surface expression (MEASURE) assay to quantify factor H binding protein expression at the surface of meningococcal serogroup B strains.Diagnostic microbiology and infectious disease · 2025Article
- Identification of a Kingella kingae factor H binding protein that is the major determinant of serum resistance.PLoS pathogens · 2025Article
- Global quantitative proteome analysis of a multi-resistantFrontiers in microbiology · 2025Article
- Factor H binding protein (FHbp): An evaluation of genotypic diversity acrossHuman vaccines & immunotherapeutics · 2024Review
- Expression, purification, and characterization of diacylated Lipo-YcjN frombioRxiv : the preprint server for biology · 2024Article
- Immune interface interference vaccines: An evolution-informed approach to anti-bacterial vaccine design.Microbial biotechnology · 2024Article
- Extensive Genetic Diversity and Epidemiological Patterns of Factor H-Binding Protein Variants amongMicroorganisms · 2024Article
- Bioinformatics Analysis of Global Diversity in Meningococcal Vaccine Antigens over the Past 10 Years: Vaccine Efficacy Prognosis.Medical sciences (Basel, Switzerland) · 2023Article
- Meningococcal factor H-binding protein: implications for disease susceptibility, virulence, and vaccines.Trends in microbiology · 2023Review
- In vaccinated individuals serum bactericidal activity against B meningococci is abrogated by C5 inhibition but not by inhibition of the alternative complement pathway.Frontiers in immunology · 2023Article
- Safety profile of MenB-FHBp vaccine among adolescents: data from surveillance of Adverse Events Following Immunization in Puglia (Italy), 2018-2020.Human vaccines & immunotherapeutics · 2022Observational
- Recent Advances in Genomics-Based Approaches for the Development of Intracellular Bacterial Pathogen Vaccines.Pharmaceutics · 2022Review
- Article
- 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
- Mimicking Native Display of CD0873 on Liposomes Augments Its Potency as an Oral Vaccine againstVaccines · 2021Article
- Development and Comparison of a Panel of Modified CS17 Fimbrial Tip Adhesin Proteins as Components for an Adhesin-Based Vaccine against EnterotoxigenicMicroorganisms · 2021Article
- Two human antibodies to a meningococcal serogroup B vaccine antigen enhance binding of complement Factor H by stabilizing the Factor H binding site.PLoS pathogens · 2021Article
106 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel antigen that induces cross-reactive bactericidal antibodies against a number of Neisseria meningitidis strains is described. This antigen, a approximately 28-kDa lipoprotein called LP2086, was first observed within a complex mixture of soluble outer membrane proteins (sOMPs) following a series of fractionation, protein purification, and proteomics steps. Approximately 95 different neisserial isolates tested positive by Western blotting and PCR screening methods for the presence of the protein and the gene encoding LP2086. The strains tested included isolates of N. meningitidis serogroups A, B, C, W135, and Y, Neisseria gonorrhoeae, and Neisseria lactamica. To better understand the microheterogeneity of this protein, the 2086 genes from 63 neisserial isolates were sequenced. Two different subfamilies of LP2086 were identified based on deduced amino acid sequence homology. A high degree of amino acid sequence similarity exists within each 2086 subfamily. The highest degree of genetic diversity was seen between the two subfamilies which share approximately 60 to 75% homology at the nucleic acid level. Flow cytometry (fluorescence-activated cell sorting) analyses and electron microscopy indicated that the LP2086 is localized on the outer surface of N. meningitidis. Antiserum produced against a single protein variant was capable of eliciting bactericidal activity against strains expressing different serosubtype antigens. Combining one recombinant lipidated 2086 (rLP2086) variant from each subfamily with two rPorA variants elicited bactericidal activity against all strains tested. The rLP2086 family of antigens are candidates worthy of further vaccine development.
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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.