A novel linear epitope at the C-terminal region of the classical swine fever virus E2 protein elicits neutralizing activity
文献类型: 外文期刊
作者: Xu, Qianru 1 ; Guo, Junqing 4 ; Ma, Fanshu 9 ; Liu, Linke 2 ; Wang, Yanan 5 ; Zhang, Shenli 2 ; Niu, Xiangxiang 2 ; Li, X 1 ;
作者机构: 1.Northwest A&F Univ, Coll Vet Med, Yangling 712100, Shaanxi, Peoples R China
2.Henan Agr Univ, Coll Vet Med, Zhengzhou 450046, Peoples R China
3.Int Associated Res Ctr Natl Anim Immunol, Zhengzhou 450046, Peoples R China
4.Henan Acad Agr Sci, Henan Prov Key Lab Anim Immunol, Zhengzhou 450002, Peoples R China
5.Jilin Univ, Coll Vet Med, Changchun 130062, Peoples R China
6.Zhengzhou Univ, Coll Publ Hlth, Zhengzhou 450001, Peoples R China
7.Henan Univ Anim Husb & Econ, Coll Vet Med, Zhengzhou 450044, Peoples R China
8.Henan Acad Agr Sci, Inst Anim Sci & Vet Med, Zhengzhou 450002, Peoples R China
9.Chinese Acad Sci, Suzhou Inst Nanotech & Nanobion, CAS Key Lab Nanobio Interface, Suzhou 215123, Peoples R China
10.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou, Jiangsu, Peoples R China
关键词: Classical swine fever virus; Neutralizing monoclonal antibodies; Linear B-cell epitope
期刊名称:INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES ( 影响因子:6.953; 五年影响因子:6.737 )
ISSN: 0141-8130
年卷期: 2021 年 189 卷
页码:
收录情况: SCI
摘要: Classical swine fever virus (CSFV) is a member of the genus Pestivirus, which causes serious economic losses. The re-emergence of the disease in Japan in 2018 has increased awareness of CSFV. In this study, Balb/c mice were immunized with plant-derived E2 protein, and four monoclonal antibodies (mAbs) 4B11, 7B3, 11A5 and 6F3 were generated. Two of these mAbs, 4B11 and 7B3, effectively blocked CSFV infection of PK-15 cells. Both mAbs recognized a novel linear epitope, (256)CLIGNTTVKVHASDER(271). The neutralizing ability of anti-CSFV serum decreased 63%, when pre-incubated with the linear peptide at 200 mu g/mL. Structural analysis showed that this linear epitope is present at the border of Domain C and Domain D on the surface of the E2 protein. Alignment of amino acid sequences showed that the epitope was conserved in different subgroups of CSFV but not in other members of the Pestivirus genus. Consistently with the analysis above, this epitope distinguished antibodies against CSFV from those against bovine viral diarrhea virus (BVDV). Our study provides an ideal candidate peptide for new vaccine design and differential diagnosis of CSFV. These findings will contribute to the control and eradication of classical swine fever.
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