Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp

López-Sagaseta, Jacinto; Beernink, Peter T.; Bianchi, Federica; Santini, Laura; Frigimelica, Elisabetta; Lucas, Alexander H.; Pizza, Mariagrazia; Bottomley, Matthew J.

doi:10.1038/s41467-018-02827-7

Title: Crystal structure reveals vaccine elicited bactericidal human antibody targeting a conserved epitope on meningococcal fHbp

Journal Article · Tue Feb 06 00:00:00 EST 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-02827-7· OSTI ID:1624073

López-Sagaseta, Jacinto ^[1];

^[2]; Bianchi, Federica ^[1]; Santini, Laura ^[1];

^[1]; Lucas, Alexander H. ^[3]; Pizza, Mariagrazia ^[1]; Bottomley, Matthew J. ^[4]

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)

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.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1624073

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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