SrasV1, PubMed, Checkpoint, bibRecord, 002B78

N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.

Identifieur interne : 002B78 ( PubMed/Checkpoint ); précédent : 002B77; suivant : 002B79

N-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 Taguchi

Source :

Journal of virology [ 0022-538X ] ; 2004.

RBID : pubmed:14671103

Descripteurs français

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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<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>
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<Abstract><AbstractText>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.</AbstractText>
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N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.

N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.

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