Receptor-induced conformational changes of murine coronavirus spike protein.
Identifieur interne : 006428 ( Main/Exploration ); précédent : 006427; suivant : 006429Receptor-induced conformational changes of murine coronavirus spike protein.
Auteurs : Shutoku Matsuyama [Japon] ; Fumihiro TaguchiSource :
- Journal of virology [ 0022-538X ] ; 2002.
Descripteurs français
- KwdFr :
- Animaux, Cartographie peptidique, Conformation des protéines, Cricetinae, Endopeptidase K, Fragments peptidiques (), Fragments peptidiques (génétique), Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (physiologie), Liaison aux protéines, Lignée cellulaire, Mutation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (physiologie), Récepteurs viraux (physiologie), Solubilité, Souris, Sous-unités de protéines, Virus de l'hépatite murine (), Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (pathogénicité), Virus de l'hépatite murine (physiologie).
- MESH :
- génétique : Fragments peptidiques, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- pathogénicité : Virus de l'hépatite murine.
- physiologie : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus de l'hépatite murine.
- Animaux, Cartographie peptidique, Conformation des protéines, Cricetinae, Endopeptidase K, Fragments peptidiques, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Liaison aux protéines, Lignée cellulaire, Mutation, Protéines de l'enveloppe virale, Solubilité, Souris, Sous-unités de protéines, Virus de l'hépatite murine.
English descriptors
- KwdEn :
- Animals, Cell Line, Cricetinae, Endopeptidase K, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Mice, Murine hepatitis virus (chemistry), Murine hepatitis virus (genetics), Murine hepatitis virus (pathogenicity), Murine hepatitis virus (physiology), Mutation, Peptide Fragments (chemistry), Peptide Fragments (genetics), Peptide Mapping, Protein Binding, Protein Conformation, Protein Subunits, Receptors, Virus (physiology), Solubility, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Peptide Fragments, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemical : Endopeptidase K, Protein Subunits, Spike Glycoprotein, Coronavirus.
- chemistry : Murine hepatitis virus.
- genetics : Murine hepatitis virus.
- pathogenicity : Murine hepatitis virus.
- physiology : Murine hepatitis virus.
- Animals, Cell Line, Cricetinae, Membrane Fusion, Mice, Mutation, Peptide Mapping, Protein Binding, Protein Conformation, Solubility.
Abstract
Although murine coronavirus mouse hepatitis virus (MHV) enters cells by virus-cell membrane fusion triggered by its spike (S) protein, it is not well known how the S protein participates in fusion events. We reported that the soluble form of MHV receptor (soMHVR) transformed a nonfusogenic S protein into a fusogenic one (F. Taguchi and S. Matsuyama, J. Virol. 76:950-958, 2002). In the present study, we demonstrate that soMHVR induces the conformational changes of the S protein, as shown by the proteinase digestion test. A cl-2 mutant, srr7, of the MHV JHM virus (JHMV) was digested with proteinase K after treatment with soMHVR, and the resultant S protein was analyzed by Western blotting using monoclonal antibody (MAb) 10G, specific for the membrane-anchored S2 subunit. A 58-kDa fragment, encompassing the two heptad repeats in S2, was detected when srr7 was digested after soMHVR treatment, while no band was seen when the virus was untreated. The appearance of the proteinase-resistant fragment was dependent on the temperature and time of srr7 incubation with soMHVR and also on the concentration of soMHVR. Coimmunoprecipitation indicated that the direct binding of soMHVR to srr7 S protein induced these conformational changes; this was also suggested by the inhibition of the changes following pretreatment of soMHVR with anti-MHVR MAb CC1. soMHVR induced conformational changes of the S proteins of wild-type (wt) JHMV cl-2, as well as revertants from srr7, srr7A and srr7B; however, a major proportion of these S proteins were resistant to proteinase K even without soMHVR treatment. The implications of this proteinase-resistant fraction are discussed. This is the first report on receptor-induced conformational changes of the membrane-anchored fragment of the coronavirus S protein.
DOI: 10.1128/jvi.76.23.11819-11826.2002
PubMed: 12414924
Affiliations:
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Le document en format XML
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type="ISSN">0022-538X</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cricetinae</term><term>Endopeptidase K</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (physiology)</term><term>Mice</term><term>Murine hepatitis virus (chemistry)</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (pathogenicity)</term><term>Murine hepatitis virus (physiology)</term><term>Mutation</term><term>Peptide Fragments (chemistry)</term><term>Peptide Fragments (genetics)</term><term>Peptide Mapping</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Subunits</term><term>Receptors, Virus (physiology)</term><term>Solubility</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cartographie peptidique</term><term>Conformation des protéines</term><term>Cricetinae</term><term>Endopeptidase K</term><term>Fragments peptidiques ()</term><term>Fragments peptidiques (génétique)</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (physiologie)</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mutation</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (physiologie)</term><term>Récepteurs viraux (physiologie)</term><term>Solubilité</term><term>Souris</term><term>Sous-unités de protéines</term><term>Virus de l'hépatite murine ()</term><term>Virus de l'hépatite murine (génétique)</term><term>Virus de l'hépatite murine (pathogénicité)</term><term>Virus de l'hépatite murine (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptide Fragments</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptide Fragments</term><term>Viral Envelope 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>Endopeptidase K</term><term>Protein Subunits</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Fragments peptidiques</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cricetinae</term><term>Membrane Fusion</term><term>Mice</term><term>Mutation</term><term>Peptide Mapping</term><term>Protein Binding</term><term>Protein Conformation</term><term>Solubility</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cartographie peptidique</term><term>Conformation des protéines</term><term>Cricetinae</term><term>Endopeptidase K</term><term>Fragments peptidiques</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mutation</term><term>Protéines de l'enveloppe virale</term><term>Solubilité</term><term>Souris</term><term>Sous-unités de protéines</term><term>Virus de l'hépatite murine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Although murine coronavirus mouse hepatitis virus (MHV) enters cells by virus-cell membrane fusion triggered by its spike (S) protein, it is not well known how the S protein participates in fusion events. We reported that the soluble form of MHV receptor (soMHVR) transformed a nonfusogenic S protein into a fusogenic one (F. Taguchi and S. Matsuyama, J. Virol. 76:950-958, 2002). In the present study, we demonstrate that soMHVR induces the conformational changes of the S protein, as shown by the proteinase digestion test. A cl-2 mutant, srr7, of the MHV JHM virus (JHMV) was digested with proteinase K after treatment with soMHVR, and the resultant S protein was analyzed by Western blotting using monoclonal antibody (MAb) 10G, specific for the membrane-anchored S2 subunit. A 58-kDa fragment, encompassing the two heptad repeats in S2, was detected when srr7 was digested after soMHVR treatment, while no band was seen when the virus was untreated. The appearance of the proteinase-resistant fragment was dependent on the temperature and time of srr7 incubation with soMHVR and also on the concentration of soMHVR. Coimmunoprecipitation indicated that the direct binding of soMHVR to srr7 S protein induced these conformational changes; this was also suggested by the inhibition of the changes following pretreatment of soMHVR with anti-MHVR MAb CC1. soMHVR induced conformational changes of the S proteins of wild-type (wt) JHMV cl-2, as well as revertants from srr7, srr7A and srr7B; however, a major proportion of these S proteins were resistant to proteinase K even without soMHVR treatment. The implications of this proteinase-resistant fraction are discussed. This is the first report on receptor-induced conformational changes of the membrane-anchored fragment of the coronavirus S protein.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement></list><tree><noCountry><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Matsuyama, Shutoku" sort="Matsuyama, Shutoku" uniqKey="Matsuyama S" first="Shutoku" last="Matsuyama">Shutoku Matsuyama</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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