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Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein.

Identifieur interne : 002D34 ( PubMed/Curation ); précédent : 002D33; suivant : 002D35

Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein.

Auteurs : Yong Xiu Yao [Royaume-Uni] ; Junyuan Ren ; Paul Heinen ; Maria Zambon ; Ian M. Jones

Source :

The Journal of infectious diseases [ 0022-1899 ] ; 2004.

RBID : pubmed:15195247

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Viral (blood), Antigens, Viral (immunology), Blotting, Western, Cells, Cultured, Flow Cytometry, Humans, Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (immunology), Recombinant Proteins (metabolism), SARS Virus (immunology), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (diagnosis), Severe Acute Respiratory Syndrome (immunology), Spike Glycoprotein, Coronavirus, Spodoptera, Trypsin (metabolism), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
MESH :
- chemical , blood : Antibodies, Viral.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Recombinant Proteins, Trypsin, Viral Envelope Proteins.
- diagnosis : Severe Acute Respiratory Syndrome.
- immunology : SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : SARS Virus.
- Animals, Blotting, Western, Cells, Cultured, Flow Cytometry, Humans, Spike Glycoprotein, Coronavirus, Spodoptera.

Abstract

Severe acute respiratory syndrome (SARS) coronavirus (SCoV) spike (S) protein is the major surface antigen of the virus and is responsible for receptor binding and the generation of neutralizing antibody. To investigate SCoV S protein, full-length and individual domains of S protein were expressed on the surface of insect cells and were characterized for cleavability and reactivity with serum samples obtained from patients during the convalescent phase of SARS. S protein could be cleaved by exogenous trypsin but not by coexpressed furin, suggesting that the protein is not normally processed during infection. Reactivity was evident by both flow cytometry and Western blot assays, but the pattern of reactivity varied according to assay and sequence of the antigen. The antibody response to SCoV S protein involves antibodies to both linear and conformational epitopes, with linear epitopes associated with the carboxyl domain and conformational epitopes associated with the amino terminal domain. Recombinant SCoV S protein appears to be a suitable antigen for the development of an efficient and sensitive diagnostic test for SARS, but our data suggest that assay format and choice of S antigen are important considerations.

DOI: 10.1086/421280
PubMed: 15195247

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) coronavirus (SCoV) spike (S) protein is the major surface antigen of the virus and is responsible for receptor binding and the generation of neutralizing antibody. To investigate SCoV S protein, full-length and individual domains of S protein were expressed on the surface of insect cells and were characterized for cleavability and reactivity with serum samples obtained from patients during the convalescent phase of SARS. S protein could be cleaved by exogenous trypsin but not by coexpressed furin, suggesting that the protein is not normally processed during infection. Reactivity was evident by both flow cytometry and Western blot assays, but the pattern of reactivity varied according to assay and sequence of the antigen. The antibody response to SCoV S protein involves antibodies to both linear and conformational epitopes, with linear epitopes associated with the carboxyl domain and conformational epitopes associated with the amino terminal domain. Recombinant SCoV S protein appears to be a suitable antigen for the development of an efficient and sensitive diagnostic test for SARS, but our data suggest that assay format and choice of S antigen are important considerations.</div>
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<Abstract><AbstractText>Severe acute respiratory syndrome (SARS) coronavirus (SCoV) spike (S) protein is the major surface antigen of the virus and is responsible for receptor binding and the generation of neutralizing antibody. To investigate SCoV S protein, full-length and individual domains of S protein were expressed on the surface of insect cells and were characterized for cleavability and reactivity with serum samples obtained from patients during the convalescent phase of SARS. S protein could be cleaved by exogenous trypsin but not by coexpressed furin, suggesting that the protein is not normally processed during infection. Reactivity was evident by both flow cytometry and Western blot assays, but the pattern of reactivity varied according to assay and sequence of the antigen. The antibody response to SCoV S protein involves antibodies to both linear and conformational epitopes, with linear epitopes associated with the carboxyl domain and conformational epitopes associated with the amino terminal domain. Recombinant SCoV S protein appears to be a suitable antigen for the development of an efficient and sensitive diagnostic test for SARS, but our data suggest that assay format and choice of S antigen are important considerations.</AbstractText>
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Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein.

Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein.

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