ArticleThe Journal of biological chemistry2009
Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 71 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
- FHbp variants among meningococci of serogroup B in Italy: Evolution and selective pressure, 2014-2017.PloS one · 2023Article
- Recent Advances in Genomics-Based Approaches for the Development of Intracellular Bacterial Pathogen Vaccines.Pharmaceutics · 2022Review
- 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
- Effect of complement Factor H on antibody repertoire and protection elicited by meningococcal capsular group B vaccines containing Factor H binding protein.Human vaccines & immunotherapeutics · 2020Article
- The Development of a Vaccine Against Meningococcus B Using Reverse Vaccinology.Frontiers in immunology · 2019Review
- Article
- Human protective response induced by meningococcus B vaccine is mediated by the synergy of multiple bactericidal epitopes.Scientific reports · 2018Article
- Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp.Nature communications · 2018Article
- Neisseria meningitidis factor H-binding protein bound to monoclonal antibody JAR5: implications for antibody synergy.The Biochemical journal · 2016Article
- The Dual Role of Lipids of the Lipoproteins in Trumenba, a Self-Adjuvanting Vaccine Against Meningococcal Meningitis B Disease.The AAPS journal · 2016Article
- FAD-I, a Fusobacterium nucleatum Cell Wall-Associated Diacylated Lipoprotein That Mediates Human Beta Defensin 2 Induction through Toll-Like Receptor-1/2 (TLR-1/2) and TLR-2/6.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
- Meningococcal B vaccination strategies and their practical application in Italy.Journal of preventive medicine and hygiene · 2015Review
- Protein Crystallography in Vaccine Research and Development.International journal of molecular sciences · 2015Review
- Structural and Computational Biology in the Design of Immunogenic Vaccine Antigens.Journal of immunology research · 2015Review
- A Mutant Library Approach to Identify Improved Meningococcal Factor H Binding Protein Vaccine Antigens.PloS one · 2015Article
- Genotypic analysis of meningococcal factor h-binding protein from non-culture clinical specimens.PloS one · 2014Article
- Article
- Role of factor H binding protein in Neisseria meningitidis virulence and its potential as a vaccine candidate to broadly protect against meningococcal disease.Microbiology and molecular biology reviews : MMBR · 2013Review
Corrections and comments
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Authors and funding
19 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LP2086 is a family of outer membrane lipoproteins from Neisseria meningitidis, which elicits bactericidal antibodies and are currently undergoing human clinical trials in a bivalent formulation where each antigen represents one of the two known LP2086 subfamilies. Here we report the NMR structure of the recombinant LP2086 variant B01, a representative of the LP2086 subfamily B. The structure reveals a novel fold composed of two domains: a "taco-shaped" N-terminal beta-sheet and a C-terminal beta-barrel connected by a linker. The structure in micellar solution is consistent with a model of LP2086 anchored to the outer membrane bilayer through its lipidated N terminus. A long flexible chain connects the folded part of the protein to the lipid anchor and acts as spacer, making both domains accessible to the host immune system. Antibodies broadly reactive against members from both subfamilies have been mapped to the N terminus. A surface of subfamily-defining residues was identified on one face of the protein, offering an explanation for the induction of subfamily-specific bactericidal antibodies.
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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.