tetano
Editor, Senior Moderator
Nat Commun
. 2022 Dec 21;13(1):7864.
doi: 10.1038/s41467-022-35586-7.
Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site
Daniel Stadlbauer[SUP] 1 [/SUP], Meagan McMahon[SUP] 1 [/SUP], Hannah L Turner[SUP] 2 [/SUP], Xueyong Zhu[SUP] 2 [/SUP], Hongquan Wan[SUP] 3 [/SUP], Juan Manuel Carreño[SUP] 1 [/SUP], George O'Dell[SUP] 1 [/SUP], Shirin Strohmeier[SUP] 1 4 [/SUP], Zain Khalil[SUP] 5 [/SUP], Marta Luksza[SUP] 5 6 [/SUP], Harm van Bakel[SUP] 5 7 [/SUP], Viviana Simon[SUP] 1 8 9 10 11 [/SUP], Ali H Ellebedy[SUP] 12 [/SUP], Ian A Wilson[SUP] 13 14 [/SUP], Andrew B Ward[SUP] 15 [/SUP], Florian Krammer[SUP] 16 17 18 [/SUP]
Affiliations
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.
. 2022 Dec 21;13(1):7864.
doi: 10.1038/s41467-022-35586-7.
Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site
Daniel Stadlbauer[SUP] 1 [/SUP], Meagan McMahon[SUP] 1 [/SUP], Hannah L Turner[SUP] 2 [/SUP], Xueyong Zhu[SUP] 2 [/SUP], Hongquan Wan[SUP] 3 [/SUP], Juan Manuel Carreño[SUP] 1 [/SUP], George O'Dell[SUP] 1 [/SUP], Shirin Strohmeier[SUP] 1 4 [/SUP], Zain Khalil[SUP] 5 [/SUP], Marta Luksza[SUP] 5 6 [/SUP], Harm van Bakel[SUP] 5 7 [/SUP], Viviana Simon[SUP] 1 8 9 10 11 [/SUP], Ali H Ellebedy[SUP] 12 [/SUP], Ian A Wilson[SUP] 13 14 [/SUP], Andrew B Ward[SUP] 15 [/SUP], Florian Krammer[SUP] 16 17 18 [/SUP]
Affiliations
- PMID: 36543789
- PMCID: PMC9772378
- DOI: 10.1038/s41467-022-35586-7
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.