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TitleAn assessment of the use of Hepatitis B Virus core protein virus-like particles to display heterologous antigens from Neisseria meningitidis.
Journal, issue, pagesVaccine, Vol. 38, Issue 16, Page 3201-3209, Year 2020
Publish dateApr 3, 2020
AuthorsSebastian Aston-Deaville / Emil Carlsson / Muhammad Saleem / Angela Thistlethwaite / Hannah Chan / Sunil Maharjan / Alessandra Facchetti / Ian M Feavers / C Alistair Siebert / Richard F Collins / Alan Roseman / Jeremy P Derrick /
PubMed AbstractNeisseria meningitidis is the causative agent of meningococcal meningitis and sepsis and remains a significant public health problem in many countries. Efforts to develop a comprehensive vaccine ...Neisseria meningitidis is the causative agent of meningococcal meningitis and sepsis and remains a significant public health problem in many countries. Efforts to develop a comprehensive vaccine against serogroup B meningococci have focused on the use of surface-exposed outer membrane proteins. Here we report the use of virus-like particles derived from the core protein of Hepatitis B Virus, HBc, to incorporate antigen domains derived from Factor H binding protein (FHbp) and the adhesin NadA. The extracellular domain of NadA was inserted into the major immunodominant region of HBc, and the C-terminal domain of FHbp at the C-terminus (CFHbp), creating a single polypeptide chain 3.7-fold larger than native HBc. Remarkably, cryoelectron microscopy revealed that the construct formed assemblies that were able to incorporate both antigens with minimal structural changes to native HBc. Electron density was weak for NadA and absent for CFHbp, partly attributable to domain flexibility. Following immunization of mice, three HBc fusions (CFHbp or NadA alone, NadA + CFHbp) were able to induce production of IgG1, IgG2a and IgG2b antibodies reactive against their respective antigens at dilutions in excess of 1:18,000. However, only HBc fusions containing NadA elicited the production of antibodies with serum bactericidal activity. It is hypothesized that this improved immune response is attributable to the adoption of a more native-like folding of crucial conformational epitopes of NadA within the chimeric VLP. This work demonstrates that HBc can incorporate insertions of large antigen domains but that maintenance of their three-dimensional structure is likely to be critical in obtaining a protective response.
External linksVaccine / PubMed:32178907 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

10316

6tik

EMDB-10316: Hepatitis B virus core protein virus-like particle displaying the antigen: extra cellular adhesion domain NadA from Neisseria meningitidis.
PDB-6tik: Hepatitis B virus core shell--virus-like particle with NadA epitope
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • neisseria meningitidis (bacteria)
  • hepatitis b virus
KeywordsVIRUS LIKE PARTICLE / Virus-like particle / VLP / antigen / NadA / Neisseria meningitidis / HBV / HBC / factor H binding protein

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