Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.
Identifieur interne : 002107 ( PubMed/Corpus ); précédent : 002106; suivant : 002108Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.
Auteurs : Gu-Choul Shin ; Yoon-Seok Chung ; In-Soo Kim ; Hae-Wol Cho ; Chun KangSource :
- Virus research [ 0168-1702 ] ; 2006.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (isolation & purification), Antibodies, Viral (immunology), Antibodies, Viral (isolation & purification), Antibody Affinity, Antigens, Viral (immunology), Cell Line, Cross Reactions, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Epitopes (immunology), Humans, Immunoblotting, Mice, Nucleocapsid Proteins (immunology), SARS Virus (immunology).
- MESH :
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Antigens, Viral, Epitopes, Nucleocapsid Proteins.
- chemical , isolation & purification : Antibodies, Monoclonal, Antibodies, Viral.
- immunology : SARS Virus.
- Animals, Antibody Affinity, Cell Line, Cross Reactions, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Humans, Immunoblotting, Mice.
Abstract
Severe acute respiratory syndrome-coronavirus nucleocapsid (SARS-CoV N) protein has been found to be important to the processes related to viral pathogenesis, such as virus replication, interference of the cell process and modulation of host immune response; detection of the antigen has been used for the early diagnosis of infection. We have used recombinant N protein expressed in insect cells to generate 17 mAbs directed against this protein. We selected five mAbs that could be used in various diagnostic assays, and all of these mAbs recognized linear epitopes. Three IgG(2b) mAbs were recognized within the N-terminus of N protein, whereas the epitope of two IgG(1) mAbs localized within the C-terminus. These mAbs were found to have significant reactivity with both non-phosphorylated and phosphorylated N proteins, which resulted in high reactivity with native N protein in virus-infected cells; however, they did not show cross-reactivity with human coronavirus. Therefore, these results suggested that these mAbs would be useful in the development of various diagnostic kits and in future studies of SARS-CoV pathology.
DOI: 10.1016/j.virusres.2006.07.004
PubMed: 16942813
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pubmed:16942813Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.</title><author><name sortKey="Shin, Gu Choul" sort="Shin, Gu Choul" uniqKey="Shin G" first="Gu-Choul" last="Shin">Gu-Choul Shin</name><affiliation><nlm:affiliation>Division of Influenza and Respiratory Viruses, Center for Infectious Disease, National Institute of Health, Korea Center for Disease Control and Prevention, 5 Nokbun-dong, Eunpyung-gu, Seoul 122-701, Republic of Korea.</nlm:affiliation></affiliation></author><author><name sortKey="Chung, Yoon Seok" sort="Chung, Yoon Seok" uniqKey="Chung Y" first="Yoon-Seok" last="Chung">Yoon-Seok Chung</name></author><author><name sortKey="Kim, In Soo" sort="Kim, In Soo" uniqKey="Kim I" first="In-Soo" last="Kim">In-Soo Kim</name></author><author><name sortKey="Cho, Hae Wol" sort="Cho, Hae Wol" uniqKey="Cho H" first="Hae-Wol" last="Cho">Hae-Wol Cho</name></author><author><name sortKey="Kang, Chun" sort="Kang, Chun" uniqKey="Kang C" first="Chun" last="Kang">Chun Kang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16942813</idno><idno type="pmid">16942813</idno><idno type="doi">10.1016/j.virusres.2006.07.004</idno><idno type="wicri:Area/PubMed/Corpus">002107</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002107</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.</title><author><name sortKey="Shin, Gu Choul" sort="Shin, Gu Choul" uniqKey="Shin G" first="Gu-Choul" last="Shin">Gu-Choul Shin</name><affiliation><nlm:affiliation>Division of Influenza and Respiratory Viruses, Center for Infectious Disease, National Institute of Health, Korea Center for Disease Control and Prevention, 5 Nokbun-dong, Eunpyung-gu, Seoul 122-701, Republic of Korea.</nlm:affiliation></affiliation></author><author><name sortKey="Chung, Yoon Seok" sort="Chung, Yoon Seok" uniqKey="Chung Y" first="Yoon-Seok" last="Chung">Yoon-Seok Chung</name></author><author><name sortKey="Kim, In Soo" sort="Kim, In Soo" uniqKey="Kim I" first="In-Soo" last="Kim">In-Soo Kim</name></author><author><name sortKey="Cho, Hae Wol" sort="Cho, Hae Wol" uniqKey="Cho H" first="Hae-Wol" last="Cho">Hae-Wol Cho</name></author><author><name sortKey="Kang, Chun" sort="Kang, Chun" uniqKey="Kang C" first="Chun" last="Kang">Chun Kang</name></author></analytic><series><title level="j">Virus research</title><idno type="ISSN">0168-1702</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Monoclonal (isolation & purification)</term><term>Antibodies, Viral (immunology)</term><term>Antibodies, Viral (isolation & purification)</term><term>Antibody Affinity</term><term>Antigens, Viral (immunology)</term><term>Cell Line</term><term>Cross Reactions</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitope Mapping</term><term>Epitopes (immunology)</term><term>Humans</term><term>Immunoblotting</term><term>Mice</term><term>Nucleocapsid Proteins (immunology)</term><term>SARS Virus (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term><term>Antigens, Viral</term><term>Epitopes</term><term>Nucleocapsid Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Antibody Affinity</term><term>Cell Line</term><term>Cross Reactions</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitope Mapping</term><term>Humans</term><term>Immunoblotting</term><term>Mice</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome-coronavirus nucleocapsid (SARS-CoV N) protein has been found to be important to the processes related to viral pathogenesis, such as virus replication, interference of the cell process and modulation of host immune response; detection of the antigen has been used for the early diagnosis of infection. We have used recombinant N protein expressed in insect cells to generate 17 mAbs directed against this protein. We selected five mAbs that could be used in various diagnostic assays, and all of these mAbs recognized linear epitopes. Three IgG(2b) mAbs were recognized within the N-terminus of N protein, whereas the epitope of two IgG(1) mAbs localized within the C-terminus. These mAbs were found to have significant reactivity with both non-phosphorylated and phosphorylated N proteins, which resulted in high reactivity with native N protein in virus-infected cells; however, they did not show cross-reactivity with human coronavirus. Therefore, these results suggested that these mAbs would be useful in the development of various diagnostic kits and in future studies of SARS-CoV pathology.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16942813</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>15</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0168-1702</ISSN><JournalIssue CitedMedium="Print"><Volume>122</Volume><Issue>1-2</Issue><PubDate><Year>2006</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Preparation and characterization of a novel monoclonal antibody specific to severe acute respiratory syndrome-coronavirus nucleocapsid protein.</ArticleTitle><Pagination><MedlinePgn>109-18</MedlinePgn></Pagination><Abstract><AbstractText>Severe acute respiratory syndrome-coronavirus nucleocapsid (SARS-CoV N) protein has been found to be important to the processes related to viral pathogenesis, such as virus replication, interference of the cell process and modulation of host immune response; detection of the antigen has been used for the early diagnosis of infection. We have used recombinant N protein expressed in insect cells to generate 17 mAbs directed against this protein. We selected five mAbs that could be used in various diagnostic assays, and all of these mAbs recognized linear epitopes. Three IgG(2b) mAbs were recognized within the N-terminus of N protein, whereas the epitope of two IgG(1) mAbs localized within the C-terminus. These mAbs were found to have significant reactivity with both non-phosphorylated and phosphorylated N proteins, which resulted in high reactivity with native N protein in virus-infected cells; however, they did not show cross-reactivity with human coronavirus. Therefore, these results suggested that these mAbs would be useful in the development of various diagnostic kits and in future studies of SARS-CoV pathology.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shin</LastName><ForeName>Gu-Choul</ForeName><Initials>GC</Initials><AffiliationInfo><Affiliation>Division of Influenza and Respiratory Viruses, Center for Infectious Disease, National Institute of Health, Korea Center for Disease Control and Prevention, 5 Nokbun-dong, Eunpyung-gu, Seoul 122-701, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chung</LastName><ForeName>Yoon-Seok</ForeName><Initials>YS</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>In-Soo</ForeName><Initials>IS</Initials></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Hae-Wol</ForeName><Initials>HW</Initials></Author><Author ValidYN="Y"><LastName>Kang</LastName><ForeName>Chun</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>08</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000914">Antibodies, Viral</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000956">Antigens, 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