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 Tan, M.
Right arrow Articles by Jiang, X.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tan, M.
Right arrow Articles by Jiang, X.

 Previous Article  |  Next Article 

Journal of Virology, June 2004, p. 6233-6242, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6233-6242.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The P Domain of Norovirus Capsid Protein Forms Dimer and Binds to Histo-Blood Group Antigen Receptors

Ming Tan,1 Rashmi S. Hegde,2 and Xi Jiang1*

Divisions of Infectious Diseases,1 Development Biology, Cincinnati Children's Hospital Medical Center, and Department of Pediatrics, College of Medicine, University of Cincinnati, Cincinnati, Ohio2

Received 28 November 2003/ Accepted 18 February 2004

Noroviruses (NVs) are the most important pathogen of epidemic nonbacterial gastroenteritis. The recent finding that NVs recognize human histo-blood group antigens (HBGAs) as receptors provided a new approach to study the pathogenesis of NVs. Using computational and site-directed mutagenesis approaches, our investigators previously identified a plausible binding pocket in the P domain of the NV capsids. In this study, we further characterize the role of the P domain in the interaction with human HBGA receptors using three NV strains representing three binding patterns. Our results show that the isolated P domain, although it did not form virus-like particles (VLPs), formed dimers, and the dimers bound HBGAs with the same patterns as those of the intact viral capsids. In contrast, the S domain, which formed small, thin-layer VLPs, did not bind A, B, or H HBGAs. A chimera containing the S domain of VA387 and the P domain of MOH revealed a binding pattern of the P donor strain (MOH). Deletion experiments revealed that an intact P domain is necessary for receptor binding. The P domain dimers are stable over a broad range of pH (2 to 11) or under strong denaturing conditions. Taken together, our results suggest that the P domain of NV contains essential elements for strain-specific binding to receptors. Further study of the P domain will provide useful information about the virus-receptor interaction. The high yield and easy production of the recombinant P protein in the Escherichia coli expression system will provide a simple approach to this goal.

* Corresponding author. Mailing address: Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, 3333 Burnet Ave., Cincinnati, OH 45229-3039. Phone: (513) 636-0119. Fax: (513) 636-7655. E-mail: jason.jiang{at}cchmc.org.

Journal of Virology, June 2004, p. 6233-6242, Vol. 78, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.12.6233-6242.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Choi, J.-M., Hutson, A. M., Estes, M. K., Prasad, B. V. V. (2008). Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proc. Natl. Acad. Sci. USA 105: 9175-9180 [Abstract] [Full Text]  
  • Bu, W., Mamedova, A., Tan, M., Xia, M., Jiang, X., Hegde, R. S. (2008). Structural Basis for the Receptor Binding Specificity of Norwalk Virus. J. Virol. 82: 5340-5347 [Abstract] [Full Text]  
  • Lochridge, V. P., Hardy, M. E. (2007). A Single-Amino-Acid Substitution in the P2 Domain of VP1 of Murine Norovirus Is Sufficient for Escape from Antibody Neutralization. J. Virol. 81: 12316-12322 [Abstract] [Full Text]  
  • Cao, S., Lou, Z., Tan, M., Chen, Y., Liu, Y., Zhang, Z., Zhang, X. C., Jiang, X., Li, X., Rao, Z. (2007). Structural Basis for the Recognition of Blood Group Trisaccharides by Norovirus. J. Virol. 81: 5949-5957 [Abstract] [Full Text]  
  • Tan, M., Meller, J., Jiang, X. (2006). C-terminal arginine cluster is essential for receptor binding of norovirus capsid protein.. J. Virol. 80: 7322-7331 [Abstract] [Full Text]  
  • Chen, R., Neill, J. D., Estes, M. K., Prasad, B. V. V. (2006). X-ray structure of a native calicivirus: Structural insights into antigenic diversity and host specificity. Proc. Natl. Acad. Sci. USA 103: 8048-8053 [Abstract] [Full Text]  
  • Tan, M., Jiang, X. (2005). The P Domain of Norovirus Capsid Protein Forms a Subviral Particle That Binds to Histo-Blood Group Antigen Receptors. J. Virol. 79: 14017-14030 [Abstract] [Full Text]  
  • Lochridge, V. P., Jutila, K. L., Graff, J. W., Hardy, M. E. (2005). Epitopes in the P2 domain of norovirus VP1 recognized by monoclonal antibodies that block cell interactions. J. Gen. Virol. 86: 2799-2806 [Abstract] [Full Text]  
  • Huang, P., Farkas, T., Zhong, W., Tan, M., Thornton, S., Morrow, A. L., Jiang, X. (2005). Norovirus and Histo-Blood Group Antigens: Demonstration of a Wide Spectrum of Strain Specificities and Classification of Two Major Binding Groups among Multiple Binding Patterns. J. Virol. 79: 6714-6722 [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»