Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY, USA.
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.
Nat Commun. 2022 Dec 21;13(1):7864. doi: 10.1038/s41467-022-35586-7.
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.
自 2016 年以来流行的当代甲型 H3N2 流感病毒在神经氨酸酶中获得了一个靠近酶活性位点的糖基化位点。在这里，我们研究了这种 S245N 糖基化位点是否由于抗原进化而影响针对保守活性位点的人源单克隆抗体的结合和功能。虽然我们发现神经氨酸酶活性位点结合抑制剂的抑制能力降低是可测量的，但这类广泛反应性的单克隆抗体在体内仍保持保护效力。
