Functional domains in the spike protein of transmissible gastroenteritis virus.
Identifieur interne : 003519 ( PubMed/Corpus ); précédent : 003518; suivant : 003520Functional domains in the spike protein of transmissible gastroenteritis virus.
Auteurs : H. Laude ; M. Godet ; S. Bernard ; J. Gelfi ; M. Duarte ; B. DelmasSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1995.
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
Links to Exploration step
pubmed:8830497Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Functional domains in the spike protein of transmissible gastroenteritis virus.</title><author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name><affiliation><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.</nlm:affiliation></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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1995">1995</date><idno type="RBID">pubmed:8830497</idno><idno type="pmid">8830497</idno><idno type="doi">10.1007/978-1-4615-1899-0_48</idno><idno type="wicri:Area/PubMed/Corpus">003519</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003519</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Functional domains in the spike protein of transmissible gastroenteritis virus.</title><author><name sortKey="Laude, H" sort="Laude, H" uniqKey="Laude H" first="H" last="Laude">H. Laude</name><affiliation><nlm:affiliation>Unité de Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.</nlm:affiliation></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="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="genetics" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Transmissible gastroenteritis virus</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Gastroenteritis, Transmissible, of Swine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid 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></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8830497</PMID><DateCompleted><Year>1996</Year><Month>10</Month><Day>16</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0065-2598</ISSN><JournalIssue CitedMedium="Print"><Volume>380</Volume><PubDate><Year>1995</Year></PubDate></JournalIssue><Title>Advances in experimental medicine and biology</Title><ISOAbbreviation>Adv. Exp. Med. Biol.</ISOAbbreviation></Journal><ArticleTitle>Functional domains in the spike protein of transmissible gastroenteritis virus.</ArticleTitle><Pagination><MedlinePgn>299-304</MedlinePgn></Pagination><Abstract><AbstractText>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. 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