Identification of a novel linear B-cell epitope using a monoclonal antibody against the carboxy terminus of the canine distemper virus nucleoprotein and sequence analysis of the identified epitope in different CDV isolates

文献类型: 外文期刊

第一作者: Yi, Li

作者: Yi, Li;Cao, Zhigang;Tong, Mingwei;Cheng, Yuening;Li, Shuang;Wang, Jianke;Lin, Peng;Sun, Yaru;Zhang, Miao;Cheng, Shipeng;Yang, Yong

作者机构:

关键词: Canine distemper virus;Nucleoprotein;Monoclonal antibody;B-cell epitope

期刊名称:VIROLOGY JOURNAL ( 影响因子:4.099; 五年影响因子:3.719 )

ISSN: 1743-422X

年卷期: 2017 年 14 卷

页码:

收录情况: SCI

摘要: Background: The Nucleoprotein (NP) is the most abundant and highly immunogenic protein in canine distemper virus (CDV), playing an important role in CDV viral replication and assembly. Results: In this study, a specific monoclonal antibody, named C8, was produced against the NP protein C terminal (amino acids 401-523). A linear N protein epitope was identified by subjecting a series of partially overlapping synthesized peptides to enzyme-linked immunosorbent assay (ELISA) analysis. The results indicated that 444GDKYPIHFNDER455 was the minimal linear epitope that could be recognized by mAb C8. Sequence alignments demonstrated that this linear epitope is less conserved among three CDV genotypes. We next analyzed the level of conservation of the defined epitope in19 Chinese CDV clinical isolates, and it has one site variation in amino acid among these CDV isolations. 2 isolates have the amino acid mutations F451L, while one has P448Ssubstitution. Phylogenetic analysis showed the two isolates with F451Lsubstitution had a closer relationship in a virulent strain ZJ-7, so the epitope may be a significant tag associated with virus virulence. Conclusion: This collection of mAb along with defined linear epitope may provide useful reagents for investigations of NP protein function and the development of CDV specific diagnostics.

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