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Title | Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 7864, Year 2022 |
Publish date | Dec 21, 2022 |
![]() | 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 / ![]() ![]() |
PubMed 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 ...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. |
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Methods | EM (single particle) |
Resolution | 14.9 Å |
Structure data | ![]() EMDB-23562: |
Source |
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