Alternative conformations of a major antigenic site on RSV F

Jones, Harrison G.; Battles, Michael B.; Lin, Chun-Chi; Bianchi, Siro; Corti, Davide; McLellan, Jason S.; Crowe, Jr., James E.

doi:10.1371/journal.ppat.1007944

Alternative conformations of a major antigenic site on RSV F

Journal Article · Mon Jul 15 00:00:00 EDT 2019 · PLoS Pathogens

DOI:https://doi.org/10.1371/journal.ppat.1007944· OSTI ID:1591911

Jones, Harrison G. ^[1]; ^[2]; Lin, Chun-Chi ^[3]; ^[4]; Corti, Davide ^[4]; ^[5]; Crowe, Jr., James E. ^[6]

Geisel School of Medicine at Dartmouth, Hanover, NH (United States); Univ. of Texas, Austin, TX (United States)
Geisel School of Medicine at Dartmouth, Hanover, NH (United States); Adimab LLC, Lebanon, NH (United States)
Geisel School of Medicine at Dartmouth, Hanover, NH (United States)
Humabs BioMed SA, Bellinzona (Switzerland)
Univ. of Texas, Austin, TX (United States)
Vanderbilt Univ., Nashville, TN (United States)

The respiratory syncytial virus (RSV) fusion (F) glycoprotein is a major target of neutralizing antibodies arising from natural infection, and antibodies that specifically bind to the prefusion conformation of RSV F generally demonstrate the greatest neutralization potency. Prefusion-stabilized RSV F variants have been engineered as vaccine antigens, but crystal structures of these variants have revealed conformational differences in a key antigenic site located at the apex of the trimer, referred to as antigenic site Ø. Currently, it is unclear if flexibility in this region is an inherent property of prefusion RSV F or if it is related to inadequate stabilization of site Ø in the engineered variants. Therefore, we set out to investigate the conformational flexibility of antigenic site Ø, as well as the ability of the human immune system to recognize alternative conformations of this site, by determining crystal structures of prefusion RSV F bound to neutralizing human-derived antibodies AM22 and RSD5. Both antibodies bound with high affinity and were specific for the prefusion conformation of RSV F. Crystal structures of the complexes revealed that the antibodies recognized distinct conformations of antigenic site Ø, each diverging at a conserved proline residue located in the middle of an α-helix. These data suggest that antigenic site Ø exists as an ensemble of conformations, with individual antibodies recognizing discrete states. Collectively, these results have implications for the refolding of pneumovirus and paramyxovirus fusion proteins and should inform development of prefusion-stabilized RSV F vaccine candidates.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: NIGMS; USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

Grant/Contract Number:: AC02-06CH11357; AC02-98CH10886

OSTI ID:: 1591911

Alternate ID(s):: OSTI ID: 1689440

Journal Information:: PLoS Pathogens, Journal Name: PLoS Pathogens Journal Issue: 7 Vol. 15; ISSN 1553-7374

Publisher:: Public Library of ScienceCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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