Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp
Abstract
Data obtained recently in the United Kingdom following a nationwide infant immunization program against serogroup B Neisseria meningitidis (MenB) reported >80% 4CMenB vaccine-mediated protection. Factor H-binding protein (fHbp) is a meningococcal virulence factor and a component of two new MenB vaccines. Here, we investigated the structural bases underlying the fHbp-dependent protective antibody response in humans, which might inform future antigen design efforts. We present the co-crystal structure of a human antibody Fab targeting fHbp. The vaccine-elicited Fab 1A12 is cross-reactive and targets an epitope highly conserved across the repertoire of three naturally occurring fHbp variants. The free Fab structure highlights conformational rearrangements occurring upon antigen binding. Importantly, 1A12 is bactericidal against MenB strains expressing fHbp from all three variants. Our results reveal important immunological features potentially contributing to the broad protection conferred by fHbp vaccination. Our studies fuel the rationale of presenting conserved protein epitopes when developing broadly protective vaccines.
- Authors:
-
[2];
[1];
- GSK Vaccines srl, Via Fiorentina 1, 53100, Siena (Italy)
- UCSF Benioff Children’s Hospital Oakland, CA (United States). Immunobiology and Vaccine Development
- UCSF Benioff Children’s Hospital Oakland, CA (United States). Immunobiology and Vaccine Development
- GSK Vaccines, Rockville, MD (United States)
- Publication Date:
- Research Org.:
- Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC)
- OSTI Identifier:
- 1624073
- Grant/Contract Number:
- AC02-05CH11231
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- English
- Subject:
- Science & Technology - Other Topics
Citation Formats
López-Sagaseta, Jacinto, Beernink, Peter T., Bianchi, Federica, Santini, Laura, Frigimelica, Elisabetta, Lucas, Alexander H., Pizza, Mariagrazia, and Bottomley, Matthew J. Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp. United States: N. p., 2018.
Web. doi:10.1038/s41467-018-02827-7.
López-Sagaseta, Jacinto, Beernink, Peter T., Bianchi, Federica, Santini, Laura, Frigimelica, Elisabetta, Lucas, Alexander H., Pizza, Mariagrazia, & Bottomley, Matthew J. Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp. United States. https://doi.org/10.1038/s41467-018-02827-7
López-Sagaseta, Jacinto, Beernink, Peter T., Bianchi, Federica, Santini, Laura, Frigimelica, Elisabetta, Lucas, Alexander H., Pizza, Mariagrazia, and Bottomley, Matthew J. Tue .
"Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp". United States. https://doi.org/10.1038/s41467-018-02827-7. https://www.osti.gov/servlets/purl/1624073.
@article{osti_1624073,
title = {Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp},
author = {López-Sagaseta, Jacinto and Beernink, Peter T. and Bianchi, Federica and Santini, Laura and Frigimelica, Elisabetta and Lucas, Alexander H. and Pizza, Mariagrazia and Bottomley, Matthew J.},
abstractNote = {Data obtained recently in the United Kingdom following a nationwide infant immunization program against serogroup B Neisseria meningitidis (MenB) reported >80% 4CMenB vaccine-mediated protection. Factor H-binding protein (fHbp) is a meningococcal virulence factor and a component of two new MenB vaccines. Here, we investigated the structural bases underlying the fHbp-dependent protective antibody response in humans, which might inform future antigen design efforts. We present the co-crystal structure of a human antibody Fab targeting fHbp. The vaccine-elicited Fab 1A12 is cross-reactive and targets an epitope highly conserved across the repertoire of three naturally occurring fHbp variants. The free Fab structure highlights conformational rearrangements occurring upon antigen binding. Importantly, 1A12 is bactericidal against MenB strains expressing fHbp from all three variants. Our results reveal important immunological features potentially contributing to the broad protection conferred by fHbp vaccination. Our studies fuel the rationale of presenting conserved protein epitopes when developing broadly protective vaccines.},
doi = {10.1038/s41467-018-02827-7},
journal = {Nature Communications},
number = 1,
volume = 9,
place = {United States},
year = {Tue Feb 06 00:00:00 EST 2018},
month = {Tue Feb 06 00:00:00 EST 2018}
}
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