This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Miura, H. S.
Right arrow Articles by Taguchi, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miura, H. S.
Right arrow Articles by Taguchi, F.

 Previous Article  |  Next Article 

Journal of Virology, January 2004, p. 216-223, Vol. 78, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.1.216-223.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

N-Terminal Domain of the Murine Coronavirus Receptor CEACAM1 Is Responsible for Fusogenic Activation and Conformational Changes of the Spike Protein

Hideka S. Miura, Keiko Nakagaki, and Fumihiro Taguchi*

National Institute of Neuroscience, NCNP, Kodaira, Tokyo 187-8502, Japan

Received 18 July 2003/ Accepted 12 September 2003

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.

* Corresponding author. Mailing address: Respiratory Viral Disease Laboratory, Department of Virology III, National Institute of Infectious Diseases, 4-7-1 Gakuen, Musashi-Murayama, Tokyo 208-0011, Japan. Phone: 81-42-561-0771. Fax: 81-42-567-5631. E-mail: ftaguchi9{at}nih.go.jp.

Journal of Virology, January 2004, p. 216-223, Vol. 78, No. 1
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.1.216-223.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Matsuyama, S., Taguchi, F. (2009). Two-Step Conformational Changes in a Coronavirus Envelope Glycoprotein Mediated by Receptor Binding and Proteolysis. J. Virol. 83: 11133-11141 [Abstract] [Full Text]  
  • Kawase, M., Shirato, K., Matsuyama, S., Taguchi, F. (2009). Protease-Mediated Entry via the Endosome of Human Coronavirus 229E. J. Virol. 83: 712-721 [Abstract] [Full Text]  
  • Eifart, P., Ludwig, K., Bottcher, C., de Haan, C. A. M., Rottier, P. J. M., Korte, T., Herrmann, A. (2007). Role of Endocytosis and Low pH in Murine Hepatitis Virus Strain A59 Cell Entry. J. Virol. 81: 10758-10768 [Abstract] [Full Text]  
  • Watanabe, R., Matsuyama, S., Taguchi, F. (2006). Receptor-independent infection of murine coronavirus: analysis by spinoculation.. J. Virol. 80: 4901-4908 [Abstract] [Full Text]  
  • Verheije, M. H., Wurdinger, T., van Beusechem, V. W., de Haan, C. A. M., Gerritsen, W. R., Rottier, P. J. M. (2006). Redirecting Coronavirus to a Nonnative Receptor through a Virus-Encoded Targeting Adapter. J. Virol. 80: 1250-1260 [Abstract] [Full Text]  
  • Wurdinger, T., Verheije, M. H., Broen, K., Bosch, B. J., Haijema, B. J., de Haan, C. A. M., van Beusechem, V. W., Gerritsen, W. R., Rottier, P. J. M. (2005). Soluble Receptor-Mediated Targeting of Mouse Hepatitis Coronavirus to the Human Epidermal Growth Factor Receptor. J. Virol. 79: 15314-15322 [Abstract] [Full Text]  
  • Fukushi, S., Mizutani, T., Saijo, M., Matsuyama, S., Miyajima, N., Taguchi, F., Itamura, S., Kurane, I., Morikawa, S. (2005). Vesicular stomatitis virus pseudotyped with severe acute respiratory syndrome coronavirus spike protein. J. Gen. Virol. 86: 2269-2274 [Abstract] [Full Text]  
  • Nakagaki, K., Nakagaki, K., Taguchi, F. (2005). Receptor-Independent Spread of a Highly Neurotropic Murine Coronavirus JHMV Strain from Initially Infected Microglial Cells in Mixed Neural Cultures. J. Virol. 79: 6102-6110 [Abstract] [Full Text]  
  • Servin, A. L. (2005). Pathogenesis of Afa/Dr Diffusely Adhering Escherichia coli. Clin. Microbiol. Rev. 18: 264-292 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»