Identification of a highly conserved and surface exposed B-cell epitope on the nucleoprotein of influenza A virus.
Identifieur interne : 000603 ( Ncbi/Checkpoint ); précédent : 000602; suivant : 000604Identification of a highly conserved and surface exposed B-cell epitope on the nucleoprotein of influenza A virus.
Auteurs : Xun Gui [République populaire de Chine] ; Pinghui Ge ; Xuliang Wang ; Kunyu Yang ; Hai Yu ; Qinjian Zhao ; Yixin Chen ; Ningshao XiaSource :
- Journal of medical virology [ 1096-9071 ] ; 2014.
Descripteurs français
- KwdFr :
- Anticorps antiviraux (immunologie), Anticorps antiviraux (isolement et purification), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (isolement et purification), Cartographie épitopique, Déterminants antigéniques des lymphocytes B (immunologie), Protéines de liaison à l'ARN (immunologie), Protéines du core viral (immunologie), Séquence conservée, Technique de Western.
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Déterminants antigéniques des lymphocytes B, Protéines de liaison à l'ARN, Protéines du core viral.
- isolement et purification : Anticorps antiviraux, Anticorps monoclonaux.
- Cartographie épitopique, Séquence conservée, Technique de Western.
English descriptors
- KwdEn :
- Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (isolation & purification), Antibodies, Viral (immunology), Antibodies, Viral (isolation & purification), Blotting, Western, Conserved Sequence, Epitope Mapping, Epitopes, B-Lymphocyte (immunology), RNA-Binding Proteins (immunology), Viral Core Proteins (immunology).
- MESH :
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Epitopes, B-Lymphocyte, RNA-Binding Proteins, Viral Core Proteins.
- chemical , isolation & purification : Antibodies, Monoclonal, Antibodies, Viral.
- Blotting, Western, Conserved Sequence, Epitope Mapping.
Abstract
Influenza virus still poses a major threat to human health worldwide. The nucleoprotein (NP) of influenza A virus plays an essential role in the viral replication and transcription and hence becomes a promising therapeutic target. NP forms a complicated conformation under native conditions and might denature when performing immunoassays such as western blot in the study of NP function. Therefore, it is useful to make an NP specific monoclonal antibody (mAb) that recognizes linear epitope instead of conformational epitope. In this study, a recombinant NP (rNP) of influenza A virus was over-expressed and used to generate a panel of anti-NP mAbs. These anti-NP mAbs were grouped into three classes based on their reactivity in Western blots. Only Class I mAb can react with linear rNP fragments. One of Class I mAb, 4D2, was characterized further by epitope mapping with a series of overlapping synthetic peptides, indicating that the 4D2 epitope is a surface exposed, linear epitope between amino acid residues 243 and 251. This epitope is highly conserved among different influenza A viruses with an identity of 98.4% (17,922/18,210). Western blot, co-immunoprecipitation, immunofluorescence, and immunohistochemistry experiments all indicated 4D2 is highly specific to NP of influenza A virus. The results demonstrated that 4D2 can be used as a research tool for functional study of NP in the replication cycle of influenza A virus. Further work is needed to understand the function and importance of this epitope.
DOI: 10.1002/jmv.23812
PubMed: 24136709
Affiliations:
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Disease, State Key Laboratory of Cellular Stress Biology, School of Life Science, Xiamen University, Xiamen, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>National Institute of Diagnostics and Vaccine Development in Infectious Disease, State Key Laboratory of Cellular Stress Biology, School of Life Science, Xiamen University, Xiamen</wicri:regionArea><wicri:noRegion>Xiamen</wicri:noRegion></affiliation></author><author><name sortKey="Ge, Pinghui" sort="Ge, Pinghui" uniqKey="Ge P" first="Pinghui" last="Ge">Pinghui Ge</name></author><author><name sortKey="Wang, Xuliang" sort="Wang, Xuliang" uniqKey="Wang X" first="Xuliang" last="Wang">Xuliang Wang</name></author><author><name sortKey="Yang, Kunyu" sort="Yang, Kunyu" uniqKey="Yang K" first="Kunyu" last="Yang">Kunyu Yang</name></author><author><name sortKey="Yu, Hai" sort="Yu, Hai" uniqKey="Yu H" first="Hai" last="Yu">Hai Yu</name></author><author><name sortKey="Zhao, Qinjian" sort="Zhao, Qinjian" uniqKey="Zhao Q" first="Qinjian" last="Zhao">Qinjian Zhao</name></author><author><name sortKey="Chen, Yixin" sort="Chen, Yixin" uniqKey="Chen Y" first="Yixin" last="Chen">Yixin Chen</name></author><author><name sortKey="Xia, Ningshao" sort="Xia, Ningshao" uniqKey="Xia N" first="Ningshao" last="Xia">Ningshao Xia</name></author></analytic><series><title level="j">Journal of medical virology</title><idno type="eISSN">1096-9071</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Monoclonal (isolation & purification)</term><term>Antibodies, Viral (immunology)</term><term>Antibodies, Viral (isolation & purification)</term><term>Blotting, Western</term><term>Conserved Sequence</term><term>Epitope Mapping</term><term>Epitopes, B-Lymphocyte (immunology)</term><term>RNA-Binding 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Monoclonal</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps monoclonaux</term><term>Déterminants antigéniques des lymphocytes B</term><term>Protéines de liaison à l'ARN</term><term>Protéines du core viral</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Anticorps antiviraux</term><term>Anticorps monoclonaux</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Blotting, Western</term><term>Conserved Sequence</term><term>Epitope Mapping</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie épitopique</term><term>Séquence conservée</term><term>Technique de Western</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Influenza virus still poses a major threat to human health worldwide. The nucleoprotein (NP) of influenza A virus plays an essential role in the viral replication and transcription and hence becomes a promising therapeutic target. NP forms a complicated conformation under native conditions and might denature when performing immunoassays such as western blot in the study of NP function. Therefore, it is useful to make an NP specific monoclonal antibody (mAb) that recognizes linear epitope instead of conformational epitope. In this study, a recombinant NP (rNP) of influenza A virus was over-expressed and used to generate a panel of anti-NP mAbs. These anti-NP mAbs were grouped into three classes based on their reactivity in Western blots. Only Class I mAb can react with linear rNP fragments. One of Class I mAb, 4D2, was characterized further by epitope mapping with a series of overlapping synthetic peptides, indicating that the 4D2 epitope is a surface exposed, linear epitope between amino acid residues 243 and 251. This epitope is highly conserved among different influenza A viruses with an identity of 98.4% (17,922/18,210). Western blot, co-immunoprecipitation, immunofluorescence, and immunohistochemistry experiments all indicated 4D2 is highly specific to NP of influenza A virus. The results demonstrated that 4D2 can be used as a research tool for functional study of NP in the replication cycle of influenza A virus. 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