Identification and antigenic epitope mapping of immunodominant region amino residues 510 to 672 on the spike protein of the severe acute respiratory syndrome coronavirus.
Identifieur interne : 002593 ( PubMed/Corpus ); précédent : 002592; suivant : 002594Identification and antigenic epitope mapping of immunodominant region amino residues 510 to 672 on the spike protein of the severe acute respiratory syndrome coronavirus.
Auteurs : Rong-Hong Hua ; Yun-Feng Wang ; Zhi-Gao Bu ; Yan-Jun Zhou ; Jin-Ying Ge ; Xi-Jun Wang ; Guang-Zhi TongSource :
- DNA and cell biology [ 1044-5498 ] ; 2005.
English descriptors
- KwdEn :
- Amino Acid Sequence, Epitope Mapping, Epitopes (immunology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Peptide Fragments (immunology), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (immunology), SARS Virus (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Recombinant Fusion Proteins, Viral Envelope Proteins.
- chemical , immunology : Epitopes, Membrane Glycoproteins, Peptide Fragments, Recombinant Fusion Proteins, Viral Envelope Proteins.
- immunology : SARS Virus.
- Amino Acid Sequence, Epitope Mapping, Spike Glycoprotein, Coronavirus.
Abstract
The severe acute respiratory syndrome (SARS) is a newly emerging human infectious disease caused by the severe acute respiratory syndrome coronavirus (SARS-CoV). The spike (S) protein of SARS-CoV is a major virion structural protein. It plays an important role in the interaction with receptors and neutralizing antibodies. In this study, the S1 domain of the spike protein and three truncated fragments were expressed by fusion with GST in a pGEX-6p-1 vector. Western blot results demonstrated that the 510-672 fragment of the S1 domain is a linear epitope dominant region. To map the antigenic epitope of this linear epitope dominant region, a set of 16 partially overlapping fragments spanning the fragment were fused with GST and expressed. Four antigenic epitopes S1C3 (539-559), S1C4 (548-567), S1C7/8 (583-606), and S1C10/11 (607-630) were identified. Immunization of mice with each of the four antigenic epitope-fused proteins revealed that all four proteins could elicit spike protein specific antisera. All of them were able to bind to the surface domain of the whole spike protein expressed by recombinant baculovirus in insect cells. Identification of antigenic epitopes of the spike protein of SARS-CoV may provide the basis for the development of immunity-based prophylactic, therapeutic, and diagnostic clinical techniques for the severe acute respiratory syndrome.
DOI: 10.1089/dna.2005.24.503
PubMed: 16101348
Links to Exploration step
pubmed:16101348Le document en format XML
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The spike (S) protein of SARS-CoV is a major virion structural protein. It plays an important role in the interaction with receptors and neutralizing antibodies. In this study, the S1 domain of the spike protein and three truncated fragments were expressed by fusion with GST in a pGEX-6p-1 vector. Western blot results demonstrated that the 510-672 fragment of the S1 domain is a linear epitope dominant region. To map the antigenic epitope of this linear epitope dominant region, a set of 16 partially overlapping fragments spanning the fragment were fused with GST and expressed. Four antigenic epitopes S1C3 (539-559), S1C4 (548-567), S1C7/8 (583-606), and S1C10/11 (607-630) were identified. Immunization of mice with each of the four antigenic epitope-fused proteins revealed that all four proteins could elicit spike protein specific antisera. All of them were able to bind to the surface domain of the whole spike protein expressed by recombinant baculovirus in insect cells. Identification of antigenic epitopes of the spike protein of SARS-CoV may provide the basis for the development of immunity-based prophylactic, therapeutic, and diagnostic clinical techniques for the severe acute respiratory syndrome.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16101348</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1044-5498</ISSN><JournalIssue CitedMedium="Print"><Volume>24</Volume><Issue>8</Issue><PubDate><Year>2005</Year><Month>Aug</Month></PubDate></JournalIssue><Title>DNA and cell biology</Title><ISOAbbreviation>DNA Cell Biol.</ISOAbbreviation></Journal><ArticleTitle>Identification and antigenic epitope mapping of immunodominant region amino residues 510 to 672 on the spike protein of the severe acute respiratory syndrome coronavirus.</ArticleTitle><Pagination><MedlinePgn>503-9</MedlinePgn></Pagination><Abstract><AbstractText>The severe acute respiratory syndrome (SARS) is a newly emerging human infectious disease caused by the severe acute respiratory syndrome coronavirus (SARS-CoV). The spike (S) protein of SARS-CoV is a major virion structural protein. It plays an important role in the interaction with receptors and neutralizing antibodies. In this study, the S1 domain of the spike protein and three truncated fragments were expressed by fusion with GST in a pGEX-6p-1 vector. Western blot results demonstrated that the 510-672 fragment of the S1 domain is a linear epitope dominant region. To map the antigenic epitope of this linear epitope dominant region, a set of 16 partially overlapping fragments spanning the fragment were fused with GST and expressed. Four antigenic epitopes S1C3 (539-559), S1C4 (548-567), S1C7/8 (583-606), and S1C10/11 (607-630) were identified. Immunization of mice with each of the four antigenic epitope-fused proteins revealed that all four proteins could elicit spike protein specific antisera. All of them were able to bind to the surface domain of the whole spike protein expressed by recombinant baculovirus in insect cells. 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