Influenza virus cause seasonal influenza epidemic and seriously sporadic influenza pandemic outbreaks. Hemagglutinin (HA) is an important target in the therapeutic treatment and diagnostic detection of the influenza virus. Variation in the sialic acid receptor binding site leads to strain‐specific binding and results in different binding modes to the host receptors. Here, we evaluated the neutralizing activity and hemagglutination inhibition activity of a prepared murine anti‐H1N1 monoclonal antibody PR8‐23. Then we identified the epitope peptide of antibody PR8‐23 by phage display technique from phage display peptide libraries. The identified epitope, 63‐IAPLQLGKCNIA‐74, containing two α‐helix and two β‐fold located at the footprint of the sialoglycan receptor on the RBS in the globular head domain of HA. It broads the growing arsenal of motifs for the amino acids on the globular head domain of HA in sialic acid receptor binding site and neutralizing antibody production.

中文翻译：

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中和抗体 PR8-23 靶向 H1N1 血凝素唾液酸聚糖受体结合位点的足迹

流感病毒引起季节性流感流行和严重的零星流感大流行暴发。血凝素（HA）是流感病毒治疗和诊断检测的重要靶点。唾液酸受体结合位点的变化导致菌株特异性结合，并导致与宿主受体的不同结合模式。在此，我们评估了制备的鼠抗 H1N1 单克隆抗体 PR8-23 的中和活性和血凝抑制活性。然后我们通过噬菌体展示技术从噬菌体展示肽库中鉴定了抗体PR8-23的表位肽。鉴定出的表位 63-IAPLQLGKCNIA-74，包含两个 α 螺旋和两个 β 折叠，位于 HA 球状头结构域中 RBS 上唾液酸聚糖受体的足迹处。它扩大了唾液酸受体结合位点中 HA 球状头结构域上氨基酸的不断增长的基序库和中和抗体的产生。