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N  -  nucleocapsid protein

Porcine hemagglutinating encephalomyelitis virus

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Disease relevance of N


High impact information on N


Anatomical context of N

  • Alanine substitution of either Arg-76 or Tyr-94 in the N-terminal domain of IBV N protein led to a significant decrease in its RNA-binding activity and a total loss of the infectivity of the viral RNA to Vero cells [7].
  • The non-glycosylated NP was used to immunize mice for hybridoma development [6].
  • The full length NP could be expressed in E. coli at very high level within inclusion bodies [6].
  • Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells [7].

Associations of N with chemical compounds

  • In contrast, mutation of amino acid Gln-74 to an alanine, which does not affect the binding activity of the N-terminal domain, showed minimal, if any, detrimental effect on the infectivity of IBV [7].

Analytical, diagnostic and therapeutic context of N


  1. Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae. Yu, I.M., Oldham, M.L., Zhang, J., Chen, J. J. Biol. Chem. (2006) [Pubmed]
  2. Delineation and modelling of a nucleolar retention signal in the coronavirus nucleocapsid protein. Reed, M.L., Dove, B.K., Jackson, R.M., Collins, R., Brooks, G., Hiscox, J.A. Traffic (2006) [Pubmed]
  3. Long-lived memory T lymphocyte responses against SARS coronavirus nucleocapsid protein in SARS-recovered patients. Peng, H., Yang, L.T., Wang, L.Y., Li, J., Huang, J., Lu, Z.Q., Koup, R.A., Bailer, R.T., Wu, C.Y. Virology (2006) [Pubmed]
  4. Mechanisms of establishment of persistent SARS-CoV-infected cells. Mizutani, T., Fukushi, S., Ishii, K., Sasaki, Y., Kenri, T., Saijo, M., Kanaji, Y., Shirota, K., Kurane, I., Morikawa, S. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  5. The crystal structure of ORF-9b, a lipid binding protein from the SARS coronavirus. Meier, C., Aricescu, A.R., Assenberg, R., Aplin, R.T., Gilbert, R.J., Grimes, J.M., Stuart, D.I. Structure (2006) [Pubmed]
  6. Copious production of SARS-CoV nucleocapsid protein employing codon optimized synthetic gene. Das, D., Suresh, M.R. J. Virol. Methods (2006) [Pubmed]
  7. Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells. Tan, Y.W., Fang, S., Fan, H., Lescar, J., Liu, D.X. Nucleic Acids Res. (2006) [Pubmed]
  8. Enhanced induction of SARS-CoV nucleocapsid protein-specific immune response using DNA vaccination followed by adenovirus boosting in BALB/c mice. Chunling, M., Kun, Y., Jian, X., Jian, Q., Hua, S., Minsheng, Z. Intervirology (2006) [Pubmed]
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