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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
RESUMEN

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