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

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

Nature communications (2022-12-22)
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
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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Donkey Anti-Guinea Pig IgG Antibody, HRP conjugate, Species Adsorbed, 1 mg/mL (Reconstituted), Chemicon®
Sigma-Aldrich
Anti-Human IgG (Fab specific)−Peroxidase antibody produced in goat, affinity isolated antibody