ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of the meningococcal vaccine antigen NadA and epitope mapping of a bactericidal antibody.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- Structural dynamics and immunogenicity of the recombinant and outer membrane vesicle-embedded Meningococcal antigen NadA.Nature communications · 2026Article
- EngineeringVaccines · 2024Review
- Article
- Analytical Insights into Protein-Alum Interactions and Their Impact on Conformational Epitope.Pharmaceutics · 2024Article
- Effective Multivalent Oriented Presentation of Meningococcal NadA Antigen Trimers by Self-Assembling Ferritin Nanoparticles.International journal of molecular sciences · 2023Article
- Editorial: Intersection of biophysical and structural approaches in vaccine design.Frontiers in molecular biosciences · 2023Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Article
- Identification of a specific surface epitope of OmpC for Escherichia coli O157:H7 with protein topology facilitated affinity mass spectrometry.Applied microbiology and biotechnology · 2021Article
- A recombinant commensal bacteria elicits heterologous antigen-specific immune responses during pharyngeal carriage.Science translational medicine · 2021Article
- Research advances in hydrogen-deuterium exchange mass spectrometry for protein epitope mapping.Analytical and bioanalytical chemistry · 2021Review
- Production, characterization, and epitope mapping of monoclonal antibodies of ribosomal protein S3 (rpS3).Animal cells and systems · 2021Article
- Immunological fingerprint of 4CMenB recombinant antigens via protein microarray reveals key immunosignatures correlating with bactericidal activity.Nature communications · 2020Article
- Immunogenicity of trimeric autotransporter adhesins and their potential as vaccine targets.Medical microbiology and immunology · 2020Review
- Article
- A simple and rapid pipeline for identification of receptor-binding sites on the surface proteins of pathogens.Scientific reports · 2020Article
- Single Domain Antibodies Targeting Receptor Binding Pockets of NadA Restrain Adhesion ofFrontiers in molecular biosciences · 2020Article
- Article
- Transcriptome analysis of human brain microvascular endothelial cells response to Neisseria meningitidis and its antigen MafA using RNA-seq.Scientific reports · 2019Article
- Cocrystal structure of meningococcal factor H binding protein variant 3 reveals a new crossprotective epitope recognized by human mAb 1E6.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
Corrections and comments
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Authors and funding
23 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Serogroup B Neisseria meningitidis (MenB) is a major cause of severe sepsis and invasive meningococcal disease, which is associated with 5-15% mortality and devastating long-term sequelae. Neisserial adhesin A (NadA), a trimeric autotransporter adhesin (TAA) that acts in adhesion to and invasion of host epithelial cells, is one of the three antigens discovered by genome mining that are part of the MenB vaccine that recently was approved by the European Medicines Agency. Here we present the crystal structure of NadA variant 5 at 2 Å resolution and transmission electron microscopy data for NadA variant 3 that is present in the vaccine. The two variants show similar overall topology with a novel TAA fold predominantly composed of trimeric coiled-coils with three protruding wing-like structures that create an unusual N-terminal head domain. Detailed mapping of the binding site of a bactericidal antibody by hydrogen/deuterium exchange MS shows that a protective conformational epitope is located in the head of NadA. These results provide information that is important for elucidating the biological function and vaccine efficacy of NadA.
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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.