Development of a monoclonal antibody recognizing novel linear neutralizing epitope on H protein of canine distemper virus vaccine strains (America-1 genotype)
文献类型： 外文期刊
作者： Wang, Wenjie 1 ; Bi, Zhenwei 1 ; Liu, Yakun 1 ; Xia, Xingxia 1 ; Qian, Jing 1 ; Tan, Yeping 1 ; Zhu, Yumei 1 ; Song, Suquan 2 ; Yan, Liping 2 ;
作者机构： 1.Jiangsu Acad Agr Sci, Minist Agr & Rural Affairs, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Nanjing 210014, Jiangsu, Peoples R China
2.Nanjing Agr Univ, Coll Vet Med, MOE Joint Int Res Lab Anim Hlth & Food Safety, Nanjing 210095, Jiangsu, Peoples R China
3.GuoTai Taizhou Ctr Technol Innovat Vet Biol, Taizhou 225300, Jiangsu, Peoples R China
关键词： Canine distemper virus; Hemagglutinin protein; Monoclonal antibody; Precise epitopes; Antigenic difference
期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）
ISSN： 0141-8130
年卷期： 2023 年 246 卷
页码：
收录情况： SCI
摘要： Canine distemper virus (CDV) is an economically important virus responsible for canine distemper (CD), a highly contagious disease that afflicts various animal species worldwide. The hemagglutinin (H) protein is the major neutralizing target of virus. Therefore, it is often considered as immunogen to prepare neutralizing antibodies. The accurate identification of neutralizing epitope will provide important antigenic information and extend the knowledge of mechanisms of virus neutralization. In this study, we generated a neutralizing monoclonal antibody (mAb) 4C6 against CDV H protein, and defined the minimal linear epitope 238DIEREFDT245, which was highly conserved in America-1 genotype of CDV strains (vaccines). The mAb 4C6 could not react with a CDV strain that had two substitutions of D238Y and R241G in the epitope, which appeared in most CDV strains of the other genotypes. Besides, a few different amino acid mutations in the epitope were also included. Collectively, the epitope 238DIEREFDT245 was variable in the other genotypes of CDV strains. The epitope 238DIEREFDT245 was exposed to the surface of CDV H protein, showing good antigenicity. These data will provide insights into structure, function and antigenicity of H protein and lay the foundation for the development of diagnostic technologies and vaccine design for CDV.
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