Antibody binding site mapping of SARS-CoV spike protein receptor-binding domain by a combination of yeast surface display and phage peptide library screening.
Identifieur interne : 001787 ( PubMed/Corpus ); précédent : 001786; suivant : 001788Antibody binding site mapping of SARS-CoV spike protein receptor-binding domain by a combination of yeast surface display and phage peptide library screening.
Auteurs : Xiaoping Zhang ; Jingxue Wang ; Kun Wen ; Zhirong Mou ; Liyun Zou ; Xiaoyan Che ; Bing Ni ; Yuzhang WuSource :
- Viral immunology [ 1557-8976 ] ; 2009.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (immunology), Antibodies, Neutralizing (immunology), Antibodies, Viral (immunology), Binding Sites, Cricetinae, Cricetulus, Epitopes (chemistry), Epitopes (immunology), Female, Lung (virology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Mice, Mice, Inbred BALB C, Molecular Sequence Data, Peptide Fragments (genetics), Peptide Fragments (immunology), Peptide Library, Protein Conformation, SARS Virus (immunology), Saccharomyces cerevisiae, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology).
- MESH :
- chemical , chemistry : Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Peptide Fragments.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Neutralizing, Antibodies, Viral, Epitopes, Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- immunology : SARS Virus.
- virology : Lung.
- Amino Acid Sequence, Animals, Binding Sites, Cricetinae, Cricetulus, Female, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Peptide Library, Protein Conformation, Saccharomyces cerevisiae, Spike Glycoprotein, Coronavirus.
Abstract
The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus (SARS-CoV) spike (S) protein plays an important role in viral infection, and is a potential major neutralizing determinant. In this study, three hybridoma cell lines secreting specific monoclonal antibodies against the RBD of the S protein were generated and their exact binding sites were identified. Using yeast surface display, the binding sites of these antibodies were defined to two linear regions on the RBD: S(337-360) and S(380-399). Using these monoclonal antibodies in phage peptide library screening identified 10 distinct mimotopes 12 amino acids in length. Sequence comparison between native epitopes and these mimotopes further confirmed the binding sites, and revealed key amino acid residues involved in antibody binding. None of these antibodies could neutralize the murine leukemia virus pseudotyped expressing the SARS-CoV spike protein (MLV/SARS-CoV). However, these mAbs could be useful in the diagnosis of SARS-CoV due to their exclusive reactivity with SARS-CoV. Furthermore, this study established a feasible platform for epitope mapping. Yeast surface display combined with phage peptide library screening provides a convenient strategy for the identification of epitope peptides from certain antigenic proteins.
DOI: 10.1089/vim.2009.0046
PubMed: 19951177
Links to Exploration step
pubmed:19951177Le document en format XML
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sort="Zou, Liyun" uniqKey="Zou L" first="Liyun" last="Zou">Liyun Zou</name></author><author><name sortKey="Che, Xiaoyan" sort="Che, Xiaoyan" uniqKey="Che X" first="Xiaoyan" last="Che">Xiaoyan Che</name></author><author><name sortKey="Ni, Bing" sort="Ni, Bing" uniqKey="Ni B" first="Bing" last="Ni">Bing Ni</name></author><author><name sortKey="Wu, Yuzhang" sort="Wu, Yuzhang" uniqKey="Wu Y" first="Yuzhang" last="Wu">Yuzhang Wu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19951177</idno><idno type="pmid">19951177</idno><idno type="doi">10.1089/vim.2009.0046</idno><idno type="wicri:Area/PubMed/Corpus">001787</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001787</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Antibody binding site mapping of SARS-CoV spike protein receptor-binding domain by a combination of yeast surface display and phage peptide library screening.</title><author><name sortKey="Zhang, Xiaoping" sort="Zhang, Xiaoping" uniqKey="Zhang X" first="Xiaoping" last="Zhang">Xiaoping Zhang</name><affiliation><nlm:affiliation>Institute of Immunology, the People's Liberation Army, Third Military Medical University, St. 30 Gaotanyan, District Shapingba, Chongqing 400038, China.</nlm:affiliation></affiliation></author><author><name sortKey="Wang, Jingxue" sort="Wang, Jingxue" uniqKey="Wang J" first="Jingxue" last="Wang">Jingxue Wang</name></author><author><name sortKey="Wen, Kun" sort="Wen, Kun" uniqKey="Wen K" first="Kun" last="Wen">Kun Wen</name></author><author><name sortKey="Mou, Zhirong" sort="Mou, Zhirong" uniqKey="Mou Z" first="Zhirong" last="Mou">Zhirong Mou</name></author><author><name sortKey="Zou, Liyun" sort="Zou, Liyun" uniqKey="Zou L" first="Liyun" last="Zou">Liyun Zou</name></author><author><name sortKey="Che, Xiaoyan" sort="Che, Xiaoyan" uniqKey="Che X" first="Xiaoyan" last="Che">Xiaoyan Che</name></author><author><name sortKey="Ni, Bing" sort="Ni, Bing" uniqKey="Ni B" first="Bing" last="Ni">Bing Ni</name></author><author><name sortKey="Wu, Yuzhang" sort="Wu, Yuzhang" uniqKey="Wu Y" first="Yuzhang" last="Wu">Yuzhang Wu</name></author></analytic><series><title level="j">Viral immunology</title><idno type="eISSN">1557-8976</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibodies, Monoclonal (immunology)</term><term>Antibodies, Neutralizing (immunology)</term><term>Antibodies, Viral (immunology)</term><term>Binding Sites</term><term>Cricetinae</term><term>Cricetulus</term><term>Epitopes (chemistry)</term><term>Epitopes (immunology)</term><term>Female</term><term>Lung (virology)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (immunology)</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term><term>Peptide Fragments (genetics)</term><term>Peptide Fragments (immunology)</term><term>Peptide Library</term><term>Protein Conformation</term><term>SARS Virus (immunology)</term><term>Saccharomyces cerevisiae</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Epitopes</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peptide Fragments</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Antibodies, Neutralizing</term><term>Antibodies, Viral</term><term>Epitopes</term><term>Membrane Glycoproteins</term><term>Peptide Fragments</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Lung</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Binding Sites</term><term>Cricetinae</term><term>Cricetulus</term><term>Female</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Molecular Sequence Data</term><term>Peptide Library</term><term>Protein Conformation</term><term>Saccharomyces cerevisiae</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus (SARS-CoV) spike (S) protein plays an important role in viral infection, and is a potential major neutralizing determinant. In this study, three hybridoma cell lines secreting specific monoclonal antibodies against the RBD of the S protein were generated and their exact binding sites were identified. Using yeast surface display, the binding sites of these antibodies were defined to two linear regions on the RBD: S(337-360) and S(380-399). Using these monoclonal antibodies in phage peptide library screening identified 10 distinct mimotopes 12 amino acids in length. Sequence comparison between native epitopes and these mimotopes further confirmed the binding sites, and revealed key amino acid residues involved in antibody binding. None of these antibodies could neutralize the murine leukemia virus pseudotyped expressing the SARS-CoV spike protein (MLV/SARS-CoV). However, these mAbs could be useful in the diagnosis of SARS-CoV due to their exclusive reactivity with SARS-CoV. Furthermore, this study established a feasible platform for epitope mapping. Yeast surface display combined with phage peptide library screening provides a convenient strategy for the identification of epitope peptides from certain antigenic proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19951177</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1557-8976</ISSN><JournalIssue CitedMedium="Internet"><Volume>22</Volume><Issue>6</Issue><PubDate><Year>2009</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Viral immunology</Title><ISOAbbreviation>Viral Immunol.</ISOAbbreviation></Journal><ArticleTitle>Antibody binding site mapping of SARS-CoV spike protein receptor-binding domain by a combination of yeast surface display and phage peptide library screening.</ArticleTitle><Pagination><MedlinePgn>407-15</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/vim.2009.0046</ELocationID><Abstract><AbstractText>The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus (SARS-CoV) spike (S) protein plays an important role in viral infection, and is a potential major neutralizing determinant. 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