Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site

Daniel Stadlbauer, Meagan McMahon, Hannah L. Turner, Xueyong Zhu, Hongquan Wan, Juan Manuel Carreño, George O’Dell, Shirin Strohmeier, Zain Khalil, Marta Luksza, Harm Bakel, Viviana Simon, Ali H. Ellebedy (), Ian A. Wilson (), Andrew B. Ward () and Florian Krammer ()
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Daniel Stadlbauer: Icahn School of Medicine at Mount Sinai
Meagan McMahon: Icahn School of Medicine at Mount Sinai
Hannah L. Turner: The Scripps Research Institute
Xueyong Zhu: The Scripps Research Institute
Hongquan Wan: Center for Biologics Evaluation and Research, Food and Drug Administration
Juan Manuel Carreño: Icahn School of Medicine at Mount Sinai
George O’Dell: Icahn School of Medicine at Mount Sinai
Shirin Strohmeier: Icahn School of Medicine at Mount Sinai
Zain Khalil: Icahn School of Medicine at Mount Sinai
Marta Luksza: Icahn School of Medicine at Mount Sinai
Harm Bakel: Icahn School of Medicine at Mount Sinai
Viviana Simon: Icahn School of Medicine at Mount Sinai
Ali H. Ellebedy: Washington University School of Medicine
Ian A. Wilson: The Scripps Research Institute
Andrew B. Ward: The Scripps Research Institute
Florian Krammer: Icahn School of Medicine at Mount Sinai

Nature Communications, 2022, vol. 13, issue 1, 1-8

Abstract: Abstract Contemporary influenza A H3N2 viruses circulating since 2016 have acquired a glycosylation site in the neuraminidase in close proximity to the enzymatic active site. Here, we investigate if this S245N glycosylation site, as a result of antigenic evolution, can impact binding and function of human monoclonal antibodies that target the conserved active site. While we find that a reduction in the inhibitory ability of neuraminidase active site binders is measurable, this class of broadly reactive monoclonal antibodies maintains protective efficacy in vivo.

Date: 2022
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DOI: 10.1038/s41467-022-35586-7

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