Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.
Identifieur interne : 000411 ( France/Analysis ); précédent : 000410; suivant : 000412Major receptor-binding and neutralization determinants are located within the same domain of the transmissible gastroenteritis virus (coronavirus) spike protein.
Auteurs : M. Godet [France] ; J. Grosclaude ; B. Delmas ; H. LaudeSource :
- Journal of virology [ 0022-538X ] ; 1994.
Descripteurs français
- KwdFr :
- Amorces ADN, Animaux, Anticorps monoclonaux, Cartographie de restriction, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (biosynthèse), Glycoprotéines membranaires (métabolisme), Lignée cellulaire, Mutagenèse dirigée, Protéines de l'enveloppe virale (biosynthèse), Protéines de l'enveloppe virale (métabolisme), Protéines recombinantes (biosynthèse), Protéines recombinantes (métabolisme), Réaction de polymérisation en chaîne, Récepteurs viraux (métabolisme), Sites de fixation, Spodoptera, Suidae, Séquence d'acides aminés, Séquence nucléotidique, Technique d'immunofluorescence, Tests de neutralisation, Transfection, Vecteurs génétiques, Virus de la gastroentérite transmissible (génétique), Virus de la gastroentérite transmissible (métabolisme), Épitopes (analyse).
- MESH :
- analyse : Épitopes.
- biosynthèse : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- génétique : Virus de la gastroentérite transmissible.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes, Récepteurs viraux, Virus de la gastroentérite transmissible.
- Amorces ADN, Animaux, Anticorps monoclonaux, Cartographie de restriction, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Lignée cellulaire, Mutagenèse dirigée, Réaction de polymérisation en chaîne, Sites de fixation, Spodoptera, Suidae, Séquence d'acides aminés, Séquence nucléotidique, Technique d'immunofluorescence, Tests de neutralisation, Transfection, Vecteurs génétiques.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Base Sequence, Binding Sites, Cell Line, DNA Primers, Epitopes (analysis), Fluorescent Antibody Technique, Genetic Vectors, Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Mutagenesis, Site-Directed, Neutralization Tests, Nucleopolyhedroviruses, Polymerase Chain Reaction, Receptors, Virus (metabolism), Recombinant Proteins (biosynthesis), Recombinant Proteins (metabolism), Restriction Mapping, Spike Glycoprotein, Coronavirus, Spodoptera, Swine, Transfection, Transmissible gastroenteritis virus (genetics), Transmissible gastroenteritis virus (metabolism), Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , analysis : Epitopes.
- chemical , biosynthesis : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- chemical : Antibodies, Monoclonal, DNA Primers, Spike Glycoprotein, Coronavirus.
- genetics : Transmissible gastroenteritis virus.
- metabolism : Transmissible gastroenteritis virus.
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Cell Line, Fluorescent Antibody Technique, Genetic Vectors, Molecular Sequence Data, Mutagenesis, Site-Directed, Neutralization Tests, Nucleopolyhedroviruses, Polymerase Chain Reaction, Restriction Mapping, Spodoptera, Swine, Transfection.
Abstract
The spike glycoprotein (S) of coronavirus, the major target for virus-neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization-mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor-binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.
PubMed: 7525985
Affiliations:
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pubmed:7525985Le document en format XML
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Grosclaude</name></author><author><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name></author><author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. 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Godet</name><affiliation wicri:level="1"><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité de Virologie et Immunologie Moléculaires, Institut National de la Recherche Agronomique, Jouy-en-Josas</wicri:regionArea><wicri:noRegion>Jouy-en-Josas</wicri:noRegion><wicri:noRegion>Jouy-en-Josas</wicri:noRegion></affiliation></author><author><name sortKey="Grosclaude, J" sort="Grosclaude, J" uniqKey="Grosclaude J" first="J" last="Grosclaude">J. Grosclaude</name></author><author><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name></author><author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="1994" type="published">1994</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</term><term>Base Sequence</term><term>Binding Sites</term><term>Cell Line</term><term>DNA Primers</term><term>Epitopes (analysis)</term><term>Fluorescent Antibody Technique</term><term>Genetic Vectors</term><term>Membrane Glycoproteins (biosynthesis)</term><term>Membrane Glycoproteins (metabolism)</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Neutralization Tests</term><term>Nucleopolyhedroviruses</term><term>Polymerase Chain Reaction</term><term>Receptors, Virus (metabolism)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (metabolism)</term><term>Restriction Mapping</term><term>Spike Glycoprotein, Coronavirus</term><term>Spodoptera</term><term>Swine</term><term>Transfection</term><term>Transmissible gastroenteritis virus (genetics)</term><term>Transmissible gastroenteritis virus (metabolism)</term><term>Viral Envelope Proteins (biosynthesis)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term><term>Animaux</term><term>Anticorps monoclonaux</term><term>Cartographie de restriction</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (biosynthèse)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Lignée cellulaire</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale (biosynthèse)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (métabolisme)</term><term>Réaction de polymérisation en chaîne</term><term>Récepteurs viraux (métabolisme)</term><term>Sites de fixation</term><term>Spodoptera</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Technique d'immunofluorescence</term><term>Tests de neutralisation</term><term>Transfection</term><term>Vecteurs génétiques</term><term>Virus de la gastroentérite transmissible (génétique)</term><term>Virus de la gastroentérite transmissible (métabolisme)</term><term>Épitopes (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term><term>DNA Primers</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Épitopes</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Virus de la gastroentérite transmissible</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Récepteurs viraux</term><term>Virus de la gastroentérite transmissible</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Binding Sites</term><term>Cell Line</term><term>Fluorescent Antibody Technique</term><term>Genetic Vectors</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Neutralization Tests</term><term>Nucleopolyhedroviruses</term><term>Polymerase Chain Reaction</term><term>Restriction Mapping</term><term>Spodoptera</term><term>Swine</term><term>Transfection</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Animaux</term><term>Anticorps monoclonaux</term><term>Cartographie de restriction</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Lignée cellulaire</term><term>Mutagenèse dirigée</term><term>Réaction de polymérisation en chaîne</term><term>Sites de fixation</term><term>Spodoptera</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Technique d'immunofluorescence</term><term>Tests de neutralisation</term><term>Transfection</term><term>Vecteurs génétiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike glycoprotein (S) of coronavirus, the major target for virus-neutralizing antibodies, is assumed to mediate the attachment of virions to the host cell. A 26-kilodalton fragment proteolytically cleaved from transmissible gastroenteritis virus (TGEV) S protein was previously shown to bear two adjacent antigenic sites, A and B, both defined by high-titer neutralizing antibodies. Recombinant baculoviruses expressing C-terminal truncations of the 26-kilodalton region were used to localize functionally important determinants in the S protein primary structure. Two overlapping 223- and 150-amino-acid-long products with serine 506 as a common N terminus expressed all of the site A and B epitopes and induced virus-binding antibodies. Coexpression of one of these truncated protein S derivatives with aminopeptidase N (APN), a cell surface molecule acting as a receptor for TGEV, led to the formation of a complex which could be immunoprecipitated by anti-S antibodies. These data provide evidence that major neutralization-mediating and receptor-binding determinants reside together within a domain of the S protein which behaves like an independent module. In spite of their ability to prevent S-APN interaction, the neutralizing antibodies appeared to recognize a preformed complex, thus indicating that antibody- and receptor-binding determinants should be essentially distinct. Together these findings bring new insight into the molecular mechanism of TGEV neutralization.</div></front></TEI><affiliations><list><country><li>France</li></country></list><tree><noCountry><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name><name sortKey="Grosclaude, J" sort="Grosclaude, J" uniqKey="Grosclaude J" first="J" last="Grosclaude">J. Grosclaude</name><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name></noCountry><country name="France"><noRegion><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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