N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.
Identifieur interne : 005229 ( Main/Exploration ); précédent : 005228; suivant : 005230N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.
Auteurs : Hideka S. Miura [Japon] ; Keiko Nakagaki ; Fumihiro TaguchiSource :
- Journal of virology [ 0022-538X ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Antigène carcinoembryonnaire, Antigènes CD (), Antigènes CD (métabolisme), Antigènes de différenciation (), Antigènes de différenciation (métabolisme), Conformation des protéines, Cricetinae, Cytométrie en flux, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Lignée cellulaire, Membrane cellulaire (métabolisme), Molécules d'adhérence cellulaire, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Relation structure-activité, Récepteurs viraux (), Récepteurs viraux (métabolisme), Tests de neutralisation, Virus de l'hépatite murine (métabolisme), Virus de l'hépatite murine (pathogénicité), Virus de l'hépatite murine (physiologie).
- MESH :
- métabolisme : Antigènes CD, Antigènes de différenciation, Glycoprotéines membranaires, Membrane cellulaire, Protéines de l'enveloppe virale, Récepteurs viraux, Virus de l'hépatite murine.
- pathogénicité : Virus de l'hépatite murine.
- physiologie : Virus de l'hépatite murine.
- Animaux, Antigène carcinoembryonnaire, Antigènes CD, Antigènes de différenciation, Conformation des protéines, Cricetinae, Cytométrie en flux, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Lignée cellulaire, Molécules d'adhérence cellulaire, Protéines de l'enveloppe virale, Relation structure-activité, Récepteurs viraux, Tests de neutralisation.
English descriptors
- KwdEn :
- Animals, Antigens, CD (chemistry), Antigens, CD (metabolism), Antigens, Differentiation (chemistry), Antigens, Differentiation (metabolism), Carcinoembryonic Antigen, Cell Adhesion Molecules, Cell Line, Cell Membrane (metabolism), Cricetinae, Flow Cytometry, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Murine hepatitis virus (metabolism), Murine hepatitis virus (pathogenicity), Murine hepatitis virus (physiology), Neutralization Tests, Protein Conformation, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus, Structure-Activity Relationship, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Antigens, CD, Antigens, Differentiation, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemical , metabolism : Antigens, CD, Antigens, Differentiation, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- metabolism : Cell Membrane, Murine hepatitis virus.
- pathogenicity : Murine hepatitis virus.
- physiology : Murine hepatitis virus.
- Animals, Carcinoembryonic Antigen, Cell Adhesion Molecules, Cell Line, Cricetinae, Flow Cytometry, Membrane Fusion, Neutralization Tests, Protein Conformation, Spike Glycoprotein, Coronavirus, Structure-Activity Relationship.
Abstract
The mouse hepatitis virus (MHV) receptor (MHVR), CEACAM1, has two different functions for MHV entry into cells: binding to MHV spike protein (S protein) and activation of the S protein to execute virus-cell membrane fusion, the latter of which is accompanied by conformational changes of the S protein. The MHVR comprising the N-terminal and fourth domains [R1(1,4)] displays these two activities, and the N domain is thought to be critical for binding to MHV. In this study, we have addressed whether or not the N domain alone is sufficient for these activities. We examined three types of soluble form MHVR (soMHVR), one consisting of the N domain alone [soR1(1)], one with the N and second domains [soR1(1,2)], and one [soR1(1,4)] expressed by recombinant baculoviruses. We assessed the abilities of these three types of soMHVR to bind to MHV, activate fusogenicity, and induce conformational changes of the S protein. All three types of soMHVR similarly bound to MHV, as examined by a solid-phase binding assay and neutralized MHV infectivity. They also activated S protein fusogenicity and induced its conformational changes with similar levels of efficiency. However, R1(1) expressed on the BHK cell surface failed to serve as a receptor in spite of a sufficient level of expression. The inability of expressed R1(1) to work as a receptor was due to the inaccessibility of virions to R1(1); however, these were accessible using the MHVR-specific monoclonal antibody CC1. These results collectively indicated that the N domain retains all biological activities necessary for receptor function.
DOI: 10.1128/jvi.78.1.216-223.2004
PubMed: 14671103
Affiliations:
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Le document en format XML
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Miura</name><affiliation wicri:level="1"><nlm:affiliation>National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187-8502, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187-8502</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Nakagaki, Keiko" sort="Nakagaki, Keiko" uniqKey="Nakagaki K" first="Keiko" last="Nakagaki">Keiko Nakagaki</name></author><author><name sortKey="Taguchi, Fumihiro" sort="Taguchi, Fumihiro" uniqKey="Taguchi F" first="Fumihiro" last="Taguchi">Fumihiro Taguchi</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antigens, CD (chemistry)</term><term>Antigens, CD (metabolism)</term><term>Antigens, Differentiation (chemistry)</term><term>Antigens, Differentiation (metabolism)</term><term>Carcinoembryonic Antigen</term><term>Cell Adhesion Molecules</term><term>Cell Line</term><term>Cell Membrane (metabolism)</term><term>Cricetinae</term><term>Flow Cytometry</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (metabolism)</term><term>Murine hepatitis virus (metabolism)</term><term>Murine hepatitis virus (pathogenicity)</term><term>Murine hepatitis virus (physiology)</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Receptors, Virus (chemistry)</term><term>Receptors, Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigène carcinoembryonnaire</term><term>Antigènes CD ()</term><term>Antigènes CD (métabolisme)</term><term>Antigènes de différenciation ()</term><term>Antigènes de différenciation (métabolisme)</term><term>Conformation des protéines</term><term>Cricetinae</term><term>Cytométrie en flux</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Lignée cellulaire</term><term>Membrane cellulaire (métabolisme)</term><term>Molécules d'adhérence cellulaire</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Relation structure-activité</term><term>Récepteurs viraux ()</term><term>Récepteurs viraux (métabolisme)</term><term>Tests de neutralisation</term><term>Virus de l'hépatite murine (métabolisme)</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>Antigens, CD</term><term>Antigens, Differentiation</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antigens, CD</term><term>Antigens, Differentiation</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigènes CD</term><term>Antigènes de différenciation</term><term>Glycoprotéines membranaires</term><term>Membrane cellulaire</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</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>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>Carcinoembryonic Antigen</term><term>Cell Adhesion Molecules</term><term>Cell Line</term><term>Cricetinae</term><term>Flow Cytometry</term><term>Membrane Fusion</term><term>Neutralization Tests</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Antigène carcinoembryonnaire</term><term>Antigènes CD</term><term>Antigènes de différenciation</term><term>Conformation des protéines</term><term>Cricetinae</term><term>Cytométrie en flux</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Lignée cellulaire</term><term>Molécules d'adhérence cellulaire</term><term>Protéines de l'enveloppe virale</term><term>Relation structure-activité</term><term>Récepteurs viraux</term><term>Tests de neutralisation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mouse hepatitis virus (MHV) receptor (MHVR), CEACAM1, has two different functions for MHV entry into cells: binding to MHV spike protein (S protein) and activation of the S protein to execute virus-cell membrane fusion, the latter of which is accompanied by conformational changes of the S protein. The MHVR comprising the N-terminal and fourth domains [R1(1,4)] displays these two activities, and the N domain is thought to be critical for binding to MHV. In this study, we have addressed whether or not the N domain alone is sufficient for these activities. We examined three types of soluble form MHVR (soMHVR), one consisting of the N domain alone [soR1(1)], one with the N and second domains [soR1(1,2)], and one [soR1(1,4)] expressed by recombinant baculoviruses. We assessed the abilities of these three types of soMHVR to bind to MHV, activate fusogenicity, and induce conformational changes of the S protein. All three types of soMHVR similarly bound to MHV, as examined by a solid-phase binding assay and neutralized MHV infectivity. They also activated S protein fusogenicity and induced its conformational changes with similar levels of efficiency. However, R1(1) expressed on the BHK cell surface failed to serve as a receptor in spite of a sufficient level of expression. The inability of expressed R1(1) to work as a receptor was due to the inaccessibility of virions to R1(1); however, these were accessible using the MHVR-specific monoclonal antibody CC1. These results collectively indicated that the N domain retains all biological activities necessary for receptor function.</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="Nakagaki, Keiko" sort="Nakagaki, Keiko" uniqKey="Nakagaki K" first="Keiko" last="Nakagaki">Keiko Nakagaki</name><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="Miura, Hideka S" sort="Miura, Hideka S" uniqKey="Miura H" first="Hideka S" last="Miura">Hideka S. 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