Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein
Identifieur interne : 005B66 ( Main/Exploration ); précédent : 005B65; suivant : 005B67Cleavage and serum reactivity of the severe acute respiratory syndrome coronavirus spike protein
Auteurs : YONG XIU YAO [Royaume-Uni] ; JUNYUAN REN [Royaume-Uni] ; Paul Heinen [Royaume-Uni] ; Maria Zambon [Royaume-Uni] ; Ian M. Jones [Royaume-Uni]Source :
- The Journal of infectious diseases [ 0022-1899 ] ; 2004.
Descripteurs français
- Pascal (Inist)
English descriptors
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.
Affiliations:
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Jones</name><affiliation wicri:level="1"><inist:fA14 i1="01"><s1>School of Animal and Microbial Sciences, University of Reading</s1><s2>Reading</s2><s3>GBR</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Royaume-Uni</country><wicri:noRegion>Reading</wicri:noRegion></affiliation></author></analytic><series><title level="j" type="main">The Journal of infectious diseases</title><title level="j" type="abbreviated">J. infect. dis.</title><idno type="ISSN">0022-1899</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">The Journal of infectious diseases</title><title level="j" type="abbreviated">J. infect. dis.</title><idno type="ISSN">0022-1899</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term><term>Infection</term><term>Microbiology</term><term>Protein</term><term>Serum</term><term>Severe acute respiratory syndrome</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Sérum</term><term>Protéine</term><term>Microbiologie</term><term>Infection</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Londres</li></region><settlement><li>Londres</li></settlement></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Yong Xiu Yao" sort="Yong Xiu Yao" uniqKey="Yong Xiu Yao" last="Yong Xiu Yao">YONG XIU YAO</name></noRegion><name sortKey="Heinen, Paul" sort="Heinen, Paul" uniqKey="Heinen P" first="Paul" last="Heinen">Paul Heinen</name><name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M." last="Jones">Ian M. Jones</name><name sortKey="Junyuan Ren" sort="Junyuan Ren" uniqKey="Junyuan Ren" last="Junyuan Ren">JUNYUAN REN</name><name sortKey="Zambon, Maria" sort="Zambon, Maria" uniqKey="Zambon M" first="Maria" last="Zambon">Maria Zambon</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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