Field of research

Biophysical and biochemical properties of the SARS-CoV nucleocapsid protein

Introduction




Severe acute respiratory syndrome (SARS) is a recently emergent disease which attacks the respiratory tract. It is caused by a novel coronavirus, SARS-CoV, which has a single-stranded RNA genome of ca. 29 kbs. The genome is encapsulated by numerous copies of the nucleocapsid (N) protein into a helical capsid. The N protein is one of the most abundant viral proteins and is highly immunogenic; its entry into host cells ellicits a variety of responses including apoptosis and cell-death. Our group focuses on the study of the structure and its relationship to the biochemical activities of the protein. We are particularly interested in how the N protein structure facilitates RNA binding and genomic RNA packaging.

Conference Posters

• Studies on the SARS coronavirus nucleocapsid protein using a hybrid approach - From structure to function (oral presentation)
  The 16th Triennial conference for the International Society of Magnetic Resonance , Oct. 14-19, 2007. Kenting, Taiwan.
  


• Structural Hierarchy of Severe Acute Respiratory Syndrome-associated Coronavirus Nucleocapsid Protein
  The 11th Symposium on Recent Advances in Biophysics, May 24-26, 2006. Taipei, Taiwan.
  


• Domain Organization and Dimer-Interface Structure of Severe Acute Respiratory Syndrome-Associated Coronavirus Nucleocapsid Protein
  First Asia-Pacific NMR Symposium, Nov. 10~11, 2005. Yokohama, Japan.
  


• Identification of A Dimer-forming Region In SARS-CoV Nucleocapsid Protein
  Fourth East Asian Biophysics Symposium, Nov. 3-6, 2003. Taipei, Taiwan.
  

Refereed Papers

• Chen, C.-Y., Chang, C.-K., Chang, Y.-W., Sue, S.-C., Bai, H.-I., Riang, L., Hsiao, C.-D., Huang, T.-H. (2007)
  Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA
  J. Mol. Bio. 368 (4): 1075-1086.
• Chang, C.-K., Sue S.-C., Yu, T.-h., Hsieh, C.-M., Tsai, C.-K., Chiang Y.-C., Lee S.-J., Hsiao, H.-H., Wu W.-J., Chang, W.-L., Lin, C.-H., Huang, T.-H. (2006)
  Modular organization of SARS coronavirus nucleocapsid protein
  J. Biomed. Sci. 13 (1): 59-72.
• Hsieh, P.-K., Chang S.-C., Huang, C-C., Lee, T.-T., Hsiao, C.-W., Kou, Y.-H., Chen, I.-Y., Chang, C.-K., Huang, T.-H., Chang, M.-F (2005)
  Assembly of severe acute respiratory syndrome coronavirus RNA packaging signal into virus-like particles is nucleocapsid dependent
  J. Virol. 79 (22): 13848-13855.
• Chang, C.-K., Sue S.-C., Yu, T.-H., Hsieh, C.-M., Tsai, C.-K., Chiang Y.-C., Lee S.-J., Hsiao, H.-H., Wu W.-J., Chang, C.-F., Huang, T.-H. (2005)
  The dimer interface of SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
  FEBS Lett. 579 (25): 5663-5668.
• Chang, C.-K., Simplaceanu, V., Ho, C. (2002)
  Effects of amino acid substitutions at beta131 on the structure and properties of hemoglobin: evidence for communication between alpha1beta1- and alpha1beta2-subunit interfaces
  Biochemistry 41 (17): 5644-5655.