SrasV1, Ncbi, Merge, bibRecord, 000536

Antigenicity and receptor-binding ability of recombinant SARS coronavirus spike protein.

Identifieur interne : 000536 ( Ncbi/Merge ); précédent : 000535; suivant : 000537

Antigenicity and receptor-binding ability of recombinant SARS coronavirus spike protein.

Auteurs : Tin-Yun Ho [Taïwan] ; Shih-Lu Wu ; Shin-Ei Cheng ; Yen-Chiao Wei ; Shan-Ping Huang ; Chien-Yun Hsiang

Source :

Biochemical and biophysical research communications [ 0006-291X ] ; 2004.

RBID : pubmed:14706633

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antigens, Viral (genetics), Base Sequence, Chlorocebus aethiops, Cloning, Molecular, DNA, Viral (genetics), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Protein Structure, Secondary, Receptors, Virus (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (metabolism), SARS Virus (genetics), SARS Virus (immunology), SARS Virus (metabolism), SARS Virus (pathogenicity), Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
MESH :
- chemical , chemistry : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , genetics : Antigens, Viral, DNA, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- immunology : SARS Virus.
- metabolism : SARS Virus.
- pathogenicity : SARS Virus.
- Amino Acid Sequence, Animals, Base Sequence, Chlorocebus aethiops, Cloning, Molecular, Humans, Molecular Sequence Data, Protein Structure, Secondary, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Vero Cells.

Abstract

Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus and causing worldwide outbreaks. SARS coronavirus (SARS-CoV) is an enveloped RNA virus, which contains several structural proteins. Among these proteins, spike (S) protein is responsible for binding to specific cellular receptors and is a major antigenic determinant, which induces neutralizing antibody. In order to analyze the antigenicity and receptor-binding ability of SARS-CoV S protein, we expressed the S protein in Escherichia coli using a pET expression vector. After the isopropyl-beta-D-thiogalactoside induction, S protein was expressed in the soluble form and purified by nickel-affinity chromatography to homogeneity. The amount of S protein recovered was 0.2-0.3mg/100ml bacterial culture. The S protein was recognized by sera from SARS patients by ELISA and Western blot, which indicated that recombinant S protein retained its antigenicity. By biotinylated ELISA and Western blot using biotin-labeled S protein as the probe, we identified 130-kDa and 140-kDa proteins in Vero cells that might be the cellular receptors responsible for SARS-CoV infection. Taken together, these results suggested that recombinant S protein exhibited the antigenicity and receptor-binding ability, and it could be a good candidate for further developing SARS vaccine and anti-SARS therapy.

DOI: 10.1016/j.bbrc.2003.11.180
PubMed: 14706633

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 003013
to stream PubMed, to step Curation: 003013
to stream PubMed, to step Checkpoint: 002E21

Links to Exploration step

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Le document en format XML

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<term>Receptors, Virus (metabolism)</term>
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<term>Recombinant Proteins (genetics)</term>
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<term>Données de séquences moléculaires</term>
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<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
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<term>Récepteurs viraux (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus and causing worldwide outbreaks. SARS coronavirus (SARS-CoV) is an enveloped RNA virus, which contains several structural proteins. Among these proteins, spike (S) protein is responsible for binding to specific cellular receptors and is a major antigenic determinant, which induces neutralizing antibody. In order to analyze the antigenicity and receptor-binding ability of SARS-CoV S protein, we expressed the S protein in Escherichia coli using a pET expression vector. After the isopropyl-beta-D-thiogalactoside induction, S protein was expressed in the soluble form and purified by nickel-affinity chromatography to homogeneity. The amount of S protein recovered was 0.2-0.3mg/100ml bacterial culture. The S protein was recognized by sera from SARS patients by ELISA and Western blot, which indicated that recombinant S protein retained its antigenicity. By biotinylated ELISA and Western blot using biotin-labeled S protein as the probe, we identified 130-kDa and 140-kDa proteins in Vero cells that might be the cellular receptors responsible for SARS-CoV infection. Taken together, these results suggested that recombinant S protein exhibited the antigenicity and receptor-binding ability, and it could be a good candidate for further developing SARS vaccine and anti-SARS therapy.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) is an emerging infectious disease associated with a novel coronavirus and causing worldwide outbreaks. SARS coronavirus (SARS-CoV) is an enveloped RNA virus, which contains several structural proteins. Among these proteins, spike (S) protein is responsible for binding to specific cellular receptors and is a major antigenic determinant, which induces neutralizing antibody. In order to analyze the antigenicity and receptor-binding ability of SARS-CoV S protein, we expressed the S protein in Escherichia coli using a pET expression vector. After the isopropyl-beta-D-thiogalactoside induction, S protein was expressed in the soluble form and purified by nickel-affinity chromatography to homogeneity. The amount of S protein recovered was 0.2-0.3mg/100ml bacterial culture. The S protein was recognized by sera from SARS patients by ELISA and Western blot, which indicated that recombinant S protein retained its antigenicity. By biotinylated ELISA and Western blot using biotin-labeled S protein as the probe, we identified 130-kDa and 140-kDa proteins in Vero cells that might be the cellular receptors responsible for SARS-CoV infection. Taken together, these results suggested that recombinant S protein exhibited the antigenicity and receptor-binding ability, and it could be a good candidate for further developing SARS vaccine and anti-SARS therapy.</AbstractText>
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Antigenicity and receptor-binding ability of recombinant SARS coronavirus spike protein.

Antigenicity and receptor-binding ability of recombinant SARS coronavirus spike protein.

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