A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface
Abstract
Here, we describe the discovery of a naturally occurring human antibody (Ab), FluA-20, that recognizes a new site of vulnerability on the hemagglutinin (HA) head domain and reacts with most influenza A viruses. Structural characterization of FluA-20 with H1 and H3 head domains revealed a novel epitope in the HA trimer interface, suggesting previously unrecognized dynamic features of the trimeric HA protein. The critical HA residues recognized by FluA-20 remain conserved across most subtypes of influenza A viruses, which explains the Ab’s extraordinary breadth. The Ab rapidly disrupted the integrity of HA protein trimers, inhibited cell-to-cell spread of virus in culture, and protected mice against challenge with viruses of H1N1, H3N2, H5N1, or H7N9 subtypes when used as prophylaxis or therapy. The FluA-20 Ab has uncovered an exceedingly conserved protective determinant in the influenza HA head domain trimer interface that is an unexpected new target for anti-influenza therapeutics and vaccines.
- Authors:
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1619329
- Alternate Identifier(s):
- OSTI ID: 1513049; OSTI ID: 1836722
- Grant/Contract Number:
- AC02-76SF00515; AC02-06CH11357
- Resource Type:
- Published Article
- Journal Name:
- Cell
- Additional Journal Information:
- Journal Name: Cell Journal Volume: 177 Journal Issue: 5; Journal ID: ISSN 0092-8674
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; influenza A virus; antibodies; viral; B-lymphocytes; antigen-antibody reactions; monoclonal; antibody-dependent cell cytotoxicity; hemagglutinin glycoproteins; influenza virus
Citation Formats
Bangaru, Sandhya, Lang, Shanshan, Schotsaert, Michael, Vanderven, Hillary A., Zhu, Xueyong, Kose, Nurgun, Bombardi, Robin, Finn, Jessica A., Kent, Stephen J., Gilchuk, Pavlo, Gilchuk, Iuliia, Turner, Hannah L., García-Sastre, Adolfo, Li, Sheng, Ward, Andrew B., Wilson, Ian A., and Crowe, Jr., James E. A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface. United States: N. p., 2019.
Web. doi:10.1016/j.cell.2019.04.011.
Bangaru, Sandhya, Lang, Shanshan, Schotsaert, Michael, Vanderven, Hillary A., Zhu, Xueyong, Kose, Nurgun, Bombardi, Robin, Finn, Jessica A., Kent, Stephen J., Gilchuk, Pavlo, Gilchuk, Iuliia, Turner, Hannah L., García-Sastre, Adolfo, Li, Sheng, Ward, Andrew B., Wilson, Ian A., & Crowe, Jr., James E. A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface. United States. https://doi.org/10.1016/j.cell.2019.04.011
Bangaru, Sandhya, Lang, Shanshan, Schotsaert, Michael, Vanderven, Hillary A., Zhu, Xueyong, Kose, Nurgun, Bombardi, Robin, Finn, Jessica A., Kent, Stephen J., Gilchuk, Pavlo, Gilchuk, Iuliia, Turner, Hannah L., García-Sastre, Adolfo, Li, Sheng, Ward, Andrew B., Wilson, Ian A., and Crowe, Jr., James E. Wed .
"A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface". United States. https://doi.org/10.1016/j.cell.2019.04.011.
@article{osti_1619329,
title = {A Site of Vulnerability on the Influenza Virus Hemagglutinin Head Domain Trimer Interface},
author = {Bangaru, Sandhya and Lang, Shanshan and Schotsaert, Michael and Vanderven, Hillary A. and Zhu, Xueyong and Kose, Nurgun and Bombardi, Robin and Finn, Jessica A. and Kent, Stephen J. and Gilchuk, Pavlo and Gilchuk, Iuliia and Turner, Hannah L. and García-Sastre, Adolfo and Li, Sheng and Ward, Andrew B. and Wilson, Ian A. and Crowe, Jr., James E.},
abstractNote = {Here, we describe the discovery of a naturally occurring human antibody (Ab), FluA-20, that recognizes a new site of vulnerability on the hemagglutinin (HA) head domain and reacts with most influenza A viruses. Structural characterization of FluA-20 with H1 and H3 head domains revealed a novel epitope in the HA trimer interface, suggesting previously unrecognized dynamic features of the trimeric HA protein. The critical HA residues recognized by FluA-20 remain conserved across most subtypes of influenza A viruses, which explains the Ab’s extraordinary breadth. The Ab rapidly disrupted the integrity of HA protein trimers, inhibited cell-to-cell spread of virus in culture, and protected mice against challenge with viruses of H1N1, H3N2, H5N1, or H7N9 subtypes when used as prophylaxis or therapy. The FluA-20 Ab has uncovered an exceedingly conserved protective determinant in the influenza HA head domain trimer interface that is an unexpected new target for anti-influenza therapeutics and vaccines.},
doi = {10.1016/j.cell.2019.04.011},
journal = {Cell},
number = 5,
volume = 177,
place = {United States},
year = {Wed May 01 00:00:00 EDT 2019},
month = {Wed May 01 00:00:00 EDT 2019}
}
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