ArticleScientific reports2018
The Bexsero Neisseria meningitidis serogroup B vaccine antigen NHBA is a high-affinity chondroitin sulfate binding protein.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Probing Glycosaminoglycan-Protein Interactions: Applications of Surface Plasmon Resonance.Biosensors · 2026Review
- Characterisation and Immunogenicity ofFrontiers in immunology · 2024Article
- Chondroitin sulfate-mediated albumin corona nanoparticles for the treatment of breast cancer.Asian journal of pharmaceutical sciences · 2021Article
- TheScience signaling · 2021Article
- Article
- TheVaccines · 2020Article
- Role of the Gonococcal Neisserial Heparin Binding Antigen in Microcolony Formation, and Serum Resistance and Adherence to Epithelial Cells.The Journal of infectious diseases · 2020Article
- The novel E. coli cell division protein, YtfB, plays a role in eukaryotic cell adhesion.Scientific reports · 2020Article
- Article
- The HMW2 adhesin of non-typeable Haemophilus influenzae is a human-adapted lectin that mediates high-affinity binding to 2-6 linked N-acetylneuraminic acid glycans.Biochemical and biophysical research communications · 2018Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Neisseria meningitidis is a Gram-negative bacterial pathogen that causes life threatening meningitis and septicemia. Neisseria Heparin Binding Antigen (NHBA) is an outer membrane protein that binds heparin and heparan sulfate and DNA. This protein is one of the four antigens in the meningococcal serogroup B vaccine Bexsero. In the current study, we sought to define the full glycan-binding repertoire of NHBA to better understand its role in meningococcal pathogenesis and vaccine efficacy. Glycan array analysis revealed binding to 28 structures by recombinant NHBA. Surface plasmon resonance was used to confirm the binding phenotype and to determine the affinity of the interactions. These studies revealed that the highest affinity binding of NHBA was with chondroitin sulfate (K
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