5NQP
Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151.
Summary for 5NQP
| Entry DOI | 10.2210/pdb5nqp/pdb |
| Descriptor | Factor H binding protein variant B16_001,Major outer membrane protein P.IA,Factor H binding protein variant B16_001, SULFATE ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| Functional Keywords | meningitis, vaccine, complement, chimeric, immune system |
| Biological source | Neisseria meningitidis More |
| Total number of polymer chains | 3 |
| Total formula weight | 89413.97 |
| Authors | Johnson, S.,Hollingshead, S.,Lea, S.M.,Tang, C.M. (deposition date: 2017-04-20, release date: 2018-02-28, Last modification date: 2024-01-17) |
| Primary citation | Hollingshead, S.,Jongerius, I.,Exley, R.M.,Johnson, S.,Lea, S.M.,Tang, C.M. Structure-based design of chimeric antigens for multivalent protein vaccines. Nat Commun, 9:1051-1051, 2018 Cited by PubMed Abstract: There is an urgent need to develop vaccines against pathogenic bacteria. However, this is often hindered by antigenic diversity and difficulties encountered manufacturing membrane proteins. Here we show how to use structure-based design to develop chimeric antigens (ChAs) for subunit vaccines. ChAs are generated against serogroup B Neisseria meningitidis (MenB), the predominant cause of meningococcal disease in wealthy countries. MenB ChAs exploit factor H binding protein (fHbp) as a molecular scaffold to display the immunogenic VR2 epitope from the integral membrane protein PorA. Structural analyses demonstrate fHbp is correctly folded and the PorA VR2 epitope adopts an immunogenic conformation. In mice, immunisation with ChAs generates fHbp and PorA antibodies that recognise the antigens expressed by clinical MenB isolates; these antibody responses correlate with protection against meningococcal disease. Application of ChAs is therefore a potentially powerful approach to develop multivalent subunit vaccines, which can be tailored to circumvent pathogen diversity. PubMed: 29535307DOI: 10.1038/s41467-018-03146-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.86 Å) |
Structure validation
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