A multifunctional human monoclonal neutralizing antibody that targets a unique conserved epitope on influenza HA

Sandhya Bangaru, Heng Zhang, Iuliia M. Gilchuk, Thomas G. Voss, Ryan P. Irving, Pavlo Gilchuk, Pranathi Matta, Xueyong Zhu, Shanshan Lang, Travis Nieusma, Juergen A. Richt, Randy A. Albrecht, Hillary A. Vanderven, Robin Bombardi, Stephen J. Kent, Andrew B. Ward, Ian A. Wilson () and James E. Crowe ()
Additional contact information
Sandhya Bangaru: Vanderbilt University Medical Center
Heng Zhang: The Scripps Research Institute
Iuliia M. Gilchuk: Vanderbilt University Medical Center
Thomas G. Voss: Vanderbilt University Medical Center
Ryan P. Irving: Vanderbilt University Medical Center
Pavlo Gilchuk: Vanderbilt University Medical Center
Pranathi Matta: Vanderbilt University Medical Center
Xueyong Zhu: The Scripps Research Institute
Shanshan Lang: The Scripps Research Institute
Travis Nieusma: The Scripps Research Institute
Juergen A. Richt: College of Veterinary Medicine, Kansas State University
Randy A. Albrecht: at Icahn School of Medicine at Mount Sina
Hillary A. Vanderven: Peter Doherty Institute for Infection and Immunity, University of Melbourne
Robin Bombardi: Vanderbilt University Medical Center
Stephen J. Kent: Peter Doherty Institute for Infection and Immunity, University of Melbourne
Andrew B. Ward: The Scripps Research Institute
Ian A. Wilson: The Scripps Research Institute
James E. Crowe: Vanderbilt University Medical Center

Nature Communications, 2018, vol. 9, issue 1, 1-15

Abstract: Abstract The high rate of antigenic drift in seasonal influenza viruses necessitates frequent changes in vaccine composition. Recent seasonal H3 vaccines do not protect against swine-origin H3N2 variant (H3N2v) strains that recently have caused severe human infections. Here, we report a human VH1-69 gene-encoded monoclonal antibody (mAb) designated H3v-47 that exhibits potent cross-reactive neutralization activity against human and swine H3N2 viruses that circulated since 1989. The crystal structure and electron microscopy reconstruction of H3v-47 Fab with the H3N2v hemagglutinin (HA) identify a unique epitope spanning the vestigial esterase and receptor-binding subdomains that is distinct from that of any known neutralizing antibody for influenza A H3 viruses. MAb H3v-47 functions largely by blocking viral egress from infected cells. Interestingly, H3v-47 also engages Fcγ receptor and mediates antibody dependent cellular cytotoxicity (ADCC). This newly identified conserved epitope can be used in design of novel immunogens for development of broadly protective H3 vaccines.

Date: 2018
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DOI: 10.1038/s41467-018-04704-9

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