ArticleJournal of virology2004
N-terminal domain of the murine coronavirus receptor CEACAM1 is responsible for fusogenic activation and conformational changes of the spike protein.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- Leveraging Artificial Intelligence and Gene Expression Analysis to Identify Some Potential Bovine Coronavirus (BCoV) Receptors and Host Cell Enzymes Potentially Involved in the Viral Replication and Tissue Tropism.International journal of molecular sciences · 2025Article
- Evaluation of RNA Secondary Stem-Loop Structures in the UTRs of Mouse Hepatitis Virus as New Therapeutic Targets.Pathogens (Basel, Switzerland) · 2024Article
- SARS-CoV-2 Spike Protein Stimulates Macropinocytosis in Murine and Human Macrophages via PKC-NADPH Oxidase Signaling.Antioxidants (Basel, Switzerland) · 2024Article
- A CRISPR/Cas9 genetically engineered organoid biobank reveals essential host factors for coronaviruses.Nature communications · 2021Article
- Spike Glycoprotein Is Central to Coronavirus Pathogenesis-Parallel Between m-CoV and SARS-CoV-2.Annals of neurosciences · 2021Review
- Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis.ACS omega · 2021Article
- Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis.bioRxiv : the preprint server for biology · 2020Article
- Article
- Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis.Scientific reports · 2018Article
- Structural and Molecular Evidence Suggesting Coronavirus-driven Evolution of Mouse Receptor.The Journal of biological chemistry · 2017Article
- Identification and characterization of a proteolytically primed form of the murine coronavirus spike proteins after fusion with the target cell.Journal of virology · 2014Article
- Review
- Mouse Hepatitis Virus Receptor as a Determinant of the Mouse Susceptibility to MHV Infection.Frontiers in microbiology · 2012Article
- Role of mouse hepatitis virus (MHV) receptor murine CEACAM1 in the resistance of mice to MHV infection: studies of mice with chimeric mCEACAM1a and mCEACAM1b.Journal of virology · 2010Article
- Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and proteolysis.Journal of virology · 2009Article
- Article
- Protease-mediated entry via the endosome of human coronavirus 229E.Journal of virology · 2009Article
- Role of endocytosis and low pH in murine hepatitis virus strain A59 cell entry.Journal of virology · 2007Article
- Heparan sulfate is a binding molecule but not a receptor for CEACAM1-independent infection of murine coronavirus.Virology · 2007Article
- Anti-SARS drug screening by molecular docking.Amino acids · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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