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Anti–influenza H7 human antibody targets antigenic site in hemagglutinin head domain interface
Jinhui Dong, … , Robert H. Carnahan, James E. Crowe Jr.
Jinhui Dong, … , Robert H. Carnahan, James E. Crowe Jr.
Published August 4, 2020
Citation Information: J Clin Invest. 2020;130(9):4734-4739. https://doi.org/10.1172/JCI136032.
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Concise Communication Immunology Infectious disease

Anti–influenza H7 human antibody targets antigenic site in hemagglutinin head domain interface

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Abstract

Although broadly protective, stem-targeted Abs against the influenza A virus hemagglutinin (HA) have been well studied, very limited information is available on Abs that broadly recognize the head domain. We determined the crystal structure of the HA protein of the avian H7N9 influenza virus in complex with a pan-H7, non-neutralizing, protective human Ab. The structure revealed a B cell epitope in the HA head domain trimer interface (TI). This discovery of a second major protective TI epitope supports a model in which uncleaved HA trimers exist on the surface of infected cells in a highly dynamic state that exposes hidden HA head domain features.

Authors

Jinhui Dong, Iuliia Gilchuk, Sheng Li, Ryan Irving, Matthew T. Goff, Hannah L. Turner, Andrew B. Ward, Robert H. Carnahan, James E. Crowe Jr.

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Figure 4

The H7-200 mAb binds a previously unrecognized HA TI epitope.

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The H7-200 mAb binds a previously unrecognized HA TI epitope.
(A) Superi...
(A) Superimposition of the H7-200 Fab–H7 HA1 complex structure and the H7.5 Fv–H7 HA and FluA-20 Fab–H3 HA head complex structures onto 1 protomer of the H7N9 HA trimer. Structures of the H3N2 HA head domain H7N9 HA and the H7N9 HA1 domain in the complexes were omitted for clarity. The H7N9 HA protomer 1, onto which the 3 complexes were superimposed, is shown in green, and the other 2 HA protomers are shown as a semitransparent surface representation in gray. (B) Models of conformational changes in the HA trimer.

Copyright © 2025 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

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