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

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.

SUBMITTER: Stadlbauer D

PROVIDER: S-EPMC9772378 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature

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

Stadlbauer Daniel D McMahon Meagan M Turner Hannah L HL Zhu Xueyong X Wan Hongquan H Carreño Juan Manuel JM O'Dell George G Strohmeier Shirin S Khalil Zain Z Luksza Marta M van Bakel Harm H Simon Viviana V Ellebedy Ali H AH Wilson Ian A IA Ward Andrew B AB Krammer Florian F

Nature communications 20221221 1

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 m ...[more]

PMID: 36543789

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