Daniel Stadlbauer, Meagan McMahon, Hannah L Turner, Xueyong Zhu, Hongquan Wan, Juan Manuel Carreño, George O'Dell, Shirin Strohmeier, Zain Khalil, Marta Luksza, Harm van Bakel, Viviana Simon, Ali H Ellebedy, Ian A Wilson, Andrew B Ward, Florian Krammer
Nature communications 2022 Dec 21Contemporary 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. © 2022. The Author(s).
Daniel Stadlbauer, Meagan McMahon, Hannah L Turner, Xueyong Zhu, Hongquan Wan, Juan Manuel Carreño, George O'Dell, Shirin Strohmeier, Zain Khalil, Marta Luksza, Harm van Bakel, Viviana Simon, Ali H Ellebedy, Ian A Wilson, Andrew B Ward, Florian Krammer. Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site. Nature communications. 2022 Dec 21;13(1):7864
PMID: 36543789
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