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Characterization of Neutralizing Monoclonal Antibodies and Identification of a Novel Conserved C-Terminal Linear Epitope on the Hemagglutinin Protein of the H9N2 Avian Influenza Virus

文献类型： 外文期刊

作者： Wang, Yanan 1 ; Li, Xueyang 2 ; Xu, Qianru 2 ; Niu, Xiangxiang 2 ; Zhang, Shenli 2 ; Qu, Xiaotian 2 ; Chu, Hongyan 2 ; Chen, Jinxuan 2 ; Shi, Qianqian 2 ; Zhang, Erqin 2 ; Zhang, Gaiping 1 ;

作者机构： 1.Jilin Univ, Coll Vet Med, Changchun 130062, Peoples R China

2.Henan Agr Univ, Coll Vet Med, Int Associated Res Ctr Natl Anim Immunol, Zhengzhou 450046, Peoples R China

3.Henan Univ, Sch Basic Med Sci, Kaifeng 475004, Peoples R China

4.Longhu Modern Immun Lab, Zhengzhou 450046, Peoples R China

5.Peking Univ, Sch Adv Agr Sci, Beijing 100871, Peoples R China

6.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China

7.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225000, Peoples R China

关键词： hemagglutinin protein; neutralizing monoclonal antibodies; linear B cell epitope; HA2

期刊名称：VIRUSES-BASEL （ 2021影响因子：5.818； 五年影响因子：5.811 ）

ISSN：

年卷期： 2022 年 14 卷 11 期

页码：

收录情况： SCI

摘要： The H9N2 avian influenza virus (AIV) remains a serious threat to the global poultry industry and public health. The hemagglutinin (HA) protein is an essential protective antigen of AIVs and a major target of neutralizing antibodies and vaccines. Therefore, in this study, we used rice-derived HA protein as an immunogen to generate monoclonal antibodies (mAbs) and screened them using an immunoperoxidase monolayer assay and indirect enzyme-linked immunosorbent assay. Eight mAbs reacted well with the recombinant H9N2 AIV and HA protein, four of which exhibited potent inhibitory activity against hemagglutination, while three showed remarkable neutralization capacities. Western blotting confirmed that two mAbs bound to the HA protein. Linear epitopes were identified using the mAbs; a novel linear epitope, (480)HKCDDQCM(487), was identified. Structural analysis revealed that the novel linear epitope is located at the C-terminus of HA2 near the disulfide bond-linked HA1 and HA2. Alignment of the amino acid sequences showed that the epitope was highly conserved among multiple H9N2 AIV strains. The results of this study provide novel insights for refining vaccine and diagnostic strategies and expand our understanding of the immune response against AIV.

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