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Gene Review:

N - nucleocapsid protein

Porcine hemagglutinating encephalomyelitis virus

Tan, Y.W. et al., Yu, I.M. et al., Das, D. et al., Peng, H. et al., Mizutani, T. et al., et al.

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Disease relevance of N

The nucleocapsid (N) protein plays an essential role in SARS-CoV genome packaging and virion assembly [1].
This finding provides structural evidence of the evolutionary link between Coronaviridae and Arteriviridae, suggesting that the N proteins of both viruses have a common origin [1].
The avian infectious bronchitis virus (IBV), coronavirus nucleocapsid (N) protein, localizes to the cytoplasm and the nucleolus [2].
The nucleocapsid (N) protein is a structural component of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) and can induce antibody responses in SARS patients during infection [3].
Crystal structure of the severe acute respiratory syndrome (SARS) coronavirus nucleocapsid protein dimerization domain reveals evolutionary linkage between corona- and arteriviridae [1].

High impact information on N

Although lacking significant sequence similarity, the dimerization domain of SARS-CoV N protein has a fold similar to that of the nucleocapsid protein of the porcine reproductive and respiratory syndrome virus [1].
The N-specific IFN-gamma(+)CD4(+) T cells were mainly composed of CD45RA(-)CCR7(+)CD62L(-) cells, whereas IFN-gamma(+)CD8(+) memory T cells were mostly contained within CD45RA(+)CCR7(-)CD62L(-) cell population [3].
Among the signaling pathways in persistently infected cells, Akt and JNK were phosphorylated in SARS-CoV-nucleocapsid (N) protein-expressing Vero E6 cells using vaccinia viral vector (DIs), strongly suggesting that N protein-induced phosphorylation of Akt and JNK are necessary to establish persistence [4].
Here we report the crystal structure of ORF-9b, an alternative open reading frame within the nucleocapsid (N) gene from the SARS coronavirus [5].
Copious production of SARS-CoV nucleocapsid protein employing codon optimized synthetic gene [6].

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

Based on its 3D structure, we used site-directed mutagenesis to identify residues essential for the RNA-binding activity of the IBV N protein and viral infectivity [7].
Enhanced induction of SARS-CoV nucleocapsid protein-specific immune response using DNA vaccination followed by adenovirus boosting in BALB/c mice [8].
In addition, the availability of the NP fragments could facilitate epitope mapping of anti-NP monoclonals for identifying suitable sandwich pairs [6].

References

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]
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]
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]
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]
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]
Copious production of SARS-CoV nucleocapsid protein employing codon optimized synthetic gene. Das, D., Suresh, M.R. J. Virol. Methods (2006) [Pubmed]
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]
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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