Functional domains in the spike protein of transmissible gastroenteritis virus.
Identifieur interne : 000409 ( France/Analysis ); précédent : 000408; suivant : 000410Functional domains in the spike protein of transmissible gastroenteritis virus.
Auteurs : H. Laude [France] ; M. Godet ; S. Bernard ; J. Gelfi ; M. Duarte ; B. DelmasSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1995.
Descripteurs français
- KwdFr :
- Animaux, Animaux nouveau-nés, Anticorps monoclonaux, Baculoviridae, Données de séquences moléculaires, Facteurs temps, Gastroentérite transmissible du porc (physiopathologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (biosynthèse), Glycoprotéines membranaires (physiologie), Lignée cellulaire, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (biosynthèse), Protéines de l'enveloppe virale (physiologie), Protéines recombinantes (biosynthèse), Protéines recombinantes (métabolisme), Récepteurs viraux (physiologie), Sites de fixation, Suidae, Séquence d'acides aminés, Tests de neutralisation, Transfection, Virulence, Virus de la gastroentérite transmissible (génétique), Virus de la gastroentérite transmissible (pathogénicité), Virus de la gastroentérite transmissible (physiologie).
- MESH :
- biosynthèse : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- génétique : Virus de la gastroentérite transmissible.
- métabolisme : Protéines recombinantes.
- pathogénicité : Virus de la gastroentérite transmissible.
- physiologie : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus de la gastroentérite transmissible.
- physiopathologie : Gastroentérite transmissible du porc.
- Animaux, Animaux nouveau-nés, Anticorps monoclonaux, Baculoviridae, Données de séquences moléculaires, Facteurs temps, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Lignée cellulaire, Protéines de l'enveloppe virale, Sites de fixation, Suidae, Séquence d'acides aminés, Tests de neutralisation, Transfection, Virulence.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Animals, Newborn, Antibodies, Monoclonal, Baculoviridae, Binding Sites, Cell Line, Gastroenteritis, Transmissible, of Swine (physiopathology), Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (physiology), Molecular Sequence Data, Neutralization Tests, Receptors, Virus (physiology), Recombinant Proteins (biosynthesis), Recombinant Proteins (metabolism), Spike Glycoprotein, Coronavirus, Swine, Time Factors, Transfection, Transmissible gastroenteritis virus (genetics), Transmissible gastroenteritis virus (pathogenicity), Transmissible gastroenteritis virus (physiology), Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (physiology), Virulence.
- MESH :
- chemical , biosynthesis : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Recombinant Proteins.
- chemical , physiology : Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemical : Antibodies, Monoclonal, Spike Glycoprotein, Coronavirus.
- genetics : Transmissible gastroenteritis virus.
- pathogenicity : Transmissible gastroenteritis virus.
- physiology : Transmissible gastroenteritis virus.
- physiopathology : Gastroenteritis, Transmissible, of Swine.
- Amino Acid Sequence, Animals, Animals, Newborn, Baculoviridae, Binding Sites, Cell Line, Molecular Sequence Data, Neutralization Tests, Swine, Time Factors, Transfection, Virulence.
Abstract
The coronavirus spike protein S is assumed to mediate essential biological functions, including recognition of target cells. Earlier studies from our and other groups identified two regions of the TGEV S (220K) protein possibly implicated in such functions. The first of these corresponds to the 224 amino acid N-terminal region which is deleted in PRCV, the respiratory variant of TGEV. We have examined the pathogenicity for the newborn piglet of a series of neutralization escape mutants encoding an S protein mutated in this region. Several amino acid changes were correlated with a dramatic loss of enterovirulence, thus indicating that crucial determinants are associated with this domain of S. The second region of potential relevance is the major neutralization domain. Baculovirus-vectored expression of 150 to 220 amino acid-long stretches encompassing this region, which is encoded by both TGEV and PRCV, was performed. The resultant recombinant proteins were shown to react with the cognate antibodies and to bind APN specifically, thus localizing the receptor-binding site on the S primary structure. Altogether these data lend support to the view that a domain of S protein structurally distinct from the receptor binding site is required for the virus to express its enteric tropism.
DOI: 10.1007/978-1-4615-1899-0_48
PubMed: 8830497
Affiliations:
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pubmed:8830497Le document en format XML
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Laude</name><affiliation wicri:level="1"><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Unité de Virologie et Immunologie Moléculaires, Jouy-en-Josas</wicri:regionArea><wicri:noRegion>Jouy-en-Josas</wicri:noRegion><wicri:noRegion>Jouy-en-Josas</wicri:noRegion></affiliation></author><author><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name></author><author><name sortKey="Bernard, S" sort="Bernard, S" uniqKey="Bernard S" first="S" last="Bernard">S. Bernard</name></author><author><name sortKey="Gelfi, J" sort="Gelfi, J" uniqKey="Gelfi J" first="J" last="Gelfi">J. Gelfi</name></author><author><name sortKey="Duarte, M" sort="Duarte, M" uniqKey="Duarte M" first="M" last="Duarte">M. Duarte</name></author><author><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name></author></analytic><series><title level="j">Advances in experimental medicine and biology</title><idno type="ISSN">0065-2598</idno><imprint><date when="1995" type="published">1995</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Animals, Newborn</term><term>Antibodies, Monoclonal</term><term>Baculoviridae</term><term>Binding Sites</term><term>Cell Line</term><term>Gastroenteritis, Transmissible, of Swine (physiopathology)</term><term>Membrane Glycoproteins (biosynthesis)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (physiology)</term><term>Molecular Sequence Data</term><term>Neutralization Tests</term><term>Receptors, Virus (physiology)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Swine</term><term>Time Factors</term><term>Transfection</term><term>Transmissible gastroenteritis virus (genetics)</term><term>Transmissible gastroenteritis virus (pathogenicity)</term><term>Transmissible gastroenteritis virus (physiology)</term><term>Viral Envelope Proteins (biosynthesis)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (physiology)</term><term>Virulence</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Animaux nouveau-nés</term><term>Anticorps monoclonaux</term><term>Baculoviridae</term><term>Données de séquences moléculaires</term><term>Facteurs temps</term><term>Gastroentérite transmissible du porc (physiopathologie)</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (biosynthèse)</term><term>Glycoprotéines membranaires (physiologie)</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (biosynthèse)</term><term>Protéines de l'enveloppe virale (physiologie)</term><term>Protéines recombinantes (biosynthèse)</term><term>Protéines recombinantes (métabolisme)</term><term>Récepteurs viraux (physiologie)</term><term>Sites de fixation</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Tests de neutralisation</term><term>Transfection</term><term>Virulence</term><term>Virus de la gastroentérite transmissible (génétique)</term><term>Virus de la gastroentérite transmissible (pathogénicité)</term><term>Virus de la gastroentérite transmissible (physiologie)</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="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Spike Glycoprotein, Coronavirus</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="métabolisme" xml:lang="fr"><term>Protéines 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Sequence</term><term>Animals</term><term>Animals, Newborn</term><term>Baculoviridae</term><term>Binding Sites</term><term>Cell Line</term><term>Molecular Sequence Data</term><term>Neutralization Tests</term><term>Swine</term><term>Time Factors</term><term>Transfection</term><term>Virulence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Animaux nouveau-nés</term><term>Anticorps monoclonaux</term><term>Baculoviridae</term><term>Données de séquences moléculaires</term><term>Facteurs temps</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Lignée cellulaire</term><term>Protéines de l'enveloppe virale</term><term>Sites de fixation</term><term>Suidae</term><term>Séquence d'acides aminés</term><term>Tests de neutralisation</term><term>Transfection</term><term>Virulence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The coronavirus spike protein S is assumed to mediate essential biological functions, including recognition of target cells. Earlier studies from our and other groups identified two regions of the TGEV S (220K) protein possibly implicated in such functions. The first of these corresponds to the 224 amino acid N-terminal region which is deleted in PRCV, the respiratory variant of TGEV. We have examined the pathogenicity for the newborn piglet of a series of neutralization escape mutants encoding an S protein mutated in this region. Several amino acid changes were correlated with a dramatic loss of enterovirulence, thus indicating that crucial determinants are associated with this domain of S. The second region of potential relevance is the major neutralization domain. Baculovirus-vectored expression of 150 to 220 amino acid-long stretches encompassing this region, which is encoded by both TGEV and PRCV, was performed. The resultant recombinant proteins were shown to react with the cognate antibodies and to bind APN specifically, thus localizing the receptor-binding site on the S primary structure. Altogether these data lend support to the view that a domain of S protein structurally distinct from the receptor binding site is required for the virus to express its enteric tropism.</div></front></TEI><affiliations><list><country><li>France</li></country></list><tree><noCountry><name sortKey="Bernard, S" sort="Bernard, S" uniqKey="Bernard S" first="S" last="Bernard">S. Bernard</name><name sortKey="Delmas, B" sort="Delmas, B" uniqKey="Delmas B" first="B" last="Delmas">B. Delmas</name><name sortKey="Duarte, M" sort="Duarte, M" uniqKey="Duarte M" first="M" last="Duarte">M. Duarte</name><name sortKey="Gelfi, J" sort="Gelfi, J" uniqKey="Gelfi J" first="J" last="Gelfi">J. Gelfi</name><name sortKey="Godet, M" sort="Godet, M" uniqKey="Godet M" first="M" last="Godet">M. Godet</name></noCountry><country name="France"><noRegion><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. 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