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
Abstract 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 term...
Main Authors: | , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2017-09-01
|
Series: | Virology Journal |
Subjects: | |
Online Access: | http://link.springer.com/article/10.1186/s12985-017-0858-6 |
_version_ | 1811203185329569792 |
---|---|
author | Li Yi Zhigang Cao Mingwei Tong Yuening Cheng Yong Yang Shuang Li Jianke Wang Peng Lin Yaru Sun Miao Zhang Shipeng Cheng |
author_facet | Li Yi Zhigang Cao Mingwei Tong Yuening Cheng Yong Yang Shuang Li Jianke Wang Peng Lin Yaru Sun Miao Zhang Shipeng Cheng |
author_sort | Li Yi |
collection | DOAJ |
description | Abstract 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. |
first_indexed | 2024-04-12T02:51:23Z |
format | Article |
id | doaj.art-0297148cd0f34dc3b0f4a72c591723cd |
institution | Directory Open Access Journal |
issn | 1743-422X |
language | English |
last_indexed | 2024-04-12T02:51:23Z |
publishDate | 2017-09-01 |
publisher | BMC |
record_format | Article |
series | Virology Journal |
spelling | doaj.art-0297148cd0f34dc3b0f4a72c591723cd2022-12-22T03:50:58ZengBMCVirology Journal1743-422X2017-09-011411910.1186/s12985-017-0858-6Identification 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 isolatesLi Yi0Zhigang Cao1Mingwei Tong2Yuening Cheng3Yong Yang4Shuang Li5Jianke Wang6Peng Lin7Yaru Sun8Miao Zhang9Shipeng Cheng10Institute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesKey Lab of Zoonosis Research, Ministry of Education Institute of Zoonosis, Jilin UniversityInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesInstitute of Special Wild Economic Animal and Plant Science, Chinese Academy of Agricultural SciencesAbstract 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.http://link.springer.com/article/10.1186/s12985-017-0858-6Canine distemper virusNucleoproteinMonoclonal antibodyB-cell epitope |
spellingShingle | Li Yi Zhigang Cao Mingwei Tong Yuening Cheng Yong Yang Shuang Li Jianke Wang Peng Lin Yaru Sun Miao Zhang Shipeng Cheng 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 Virology Journal Canine distemper virus Nucleoprotein Monoclonal antibody B-cell epitope |
title | 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 |
title_full | 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 |
title_fullStr | 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 |
title_full_unstemmed | 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 |
title_short | 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 |
title_sort | 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 |
topic | Canine distemper virus Nucleoprotein Monoclonal antibody B-cell epitope |
url | http://link.springer.com/article/10.1186/s12985-017-0858-6 |
work_keys_str_mv | AT liyi identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT zhigangcao identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT mingweitong identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT yueningcheng identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT yongyang identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT shuangli identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT jiankewang identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT penglin identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT yarusun identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT miaozhang identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates AT shipengcheng identificationofanovellinearbcellepitopeusingamonoclonalantibodyagainstthecarboxyterminusofthecaninedistempervirusnucleoproteinandsequenceanalysisoftheidentifiedepitopeindifferentcdvisolates |