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N  -  nucleocapsid protein

Human coronavirus OC43

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Disease relevance of N


High impact information on N


Chemical compound and disease context of N

  • Here, we characterized temporal changes in N protein-specific and S glycoprotein-specific neutralizing antibody (Nab) responses in infected patients who have either recovered from or succumbed to SARS-CoV infection [7].
  • This plasmid containing the N gene was recombined with in a BaculoDirecttrade mark baculovirus DNA designed in order to express N protein in fusion with a C-terminal polyhistidine tag containing V5 epitope [8].

Biological context of N


Anatomical context of N

  • Five independent T-cell clones recognized three separate N-protein domains: 1-133, 134-249, and 250-306 [13].
  • Binding of N protein also occurs to membranes in the absence of MHV matrix (M) protein which is known to interact with the N protein [14].
  • Binding of N protein to membranes of mouse fibroblast L-2 cells is very specific and occurs under conditions in which no other viral or cellular proteins show detectable binding [14].
  • The HE and S glycoproteins were recognized earliest by the bovine immune system while the N protein induced antibody responses during the later stage of initial infection and the early stage of reinfection [15].
  • Analysis of synthesized N protein in a nondenaturing gel system showed that it bound in vitro to an endogenous RNA in the reticulocyte lysate but not to its own mRNA [16].

Associations of N with chemical compounds

  • The N protein was also shown to bind directly to phospholipid liposomes containing cardiolipin as well as to liposomes containing total lipids extracted from mouse L-2 cells [14].
  • Purified N protein was cleaved with formic acid to determine which domain interacts with the leader RNA sequence [17].
  • Recovered patients were found to have higher and sustainable levels of both N protein-specific and S glycoprotein-specific Nab responses, suggesting that antibody responses likely play an important role in determining the ultimate disease outcome of SARS-CoV-infected patients [7].
  • Recombinant N protein was extracted from infected cells, analysed by SDS-PAGE and Western blot, and purified by Ni(2+) affinity procedure [8].

Physical interactions of N

  • Pulse-labeling experiments showed that newly synthesized, unglycosylated M protein interacted with N protein in a pre-Golgi compartment, which is part of the MHV budding site [18].

Other interactions of N

  • Analysis of second-site revertants of MDelta2 revealed mutations in the carboxy-terminal region of the N protein that compensated for the defect in the M protein [2].
  • By contrast, a VV recombinant encoding a variant non fusogenic S-protein or the N-protein was not capable conferring protection [19].

Analytical, diagnostic and therapeutic context of N

  • The N protein of Alb4 was found to be smaller than its wild-type counterpart, and sequence analysis of the Alb4 N gene revealed that it contains an internal deletion of 87 nucleotides, producing an in-frame deletion of 29 amino acids [20].
  • Chemical cross-linking and gel-filtration analyses indicated that the residues 283-422 of the SARS-CoV N protein have multimeric ability, although the full-length N protein is prone to exist predominantly as dimers [21].
  • All of the Mab recognized both native protein and full-length N protein expressed in this vector by both Western blot and enzyme-linked immunoabsorbent assays (ELISA), indicating that they recognized linear epitopes [22].
  • When analysed by ELISA or by immunofluorescence only the antibody response to the N protein was significant; weak responses or no detectable response at all were found for S and M, respectively [23].
  • Using previously described BCV primers, the N protein gene of isolate NC99 was amplified by a reverse transcriptase PCR (RT-PCR) procedure [24].


  1. Nucleocapsid-independent specific viral RNA packaging via viral envelope protein and viral RNA signal. Narayanan, K., Chen, C.J., Maeda, J., Makino, S. J. Virol. (2003) [Pubmed]
  2. A major determinant for membrane protein interaction localizes to the carboxy-terminal domain of the mouse coronavirus nucleocapsid protein. Hurst, K.R., Kuo, L., Koetzner, C.A., Ye, R., Hsue, B., Masters, P.S. J. Virol. (2005) [Pubmed]
  3. 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]
  4. Antigenic and genomic relationships among turkey and bovine enteric coronaviruses. Dea, S., Verbeek, A.J., Tijssen, P. J. Virol. (1990) [Pubmed]
  5. Intracellular localization of the severe acute respiratory syndrome coronavirus nucleocapsid protein: absence of nucleolar accumulation during infection and after expression as a recombinant protein in vero cells. Rowland, R.R., Chauhan, V., Fang, Y., Pekosz, A., Kerrigan, M., Burton, M.D. J. Virol. (2005) [Pubmed]
  6. Induction of prothrombinase fgl2 by the nucleocapsid protein of virulent mouse hepatitis virus is dependent on host hepatic nuclear factor-4 alpha. Ning, Q., Lakatoo, S., Liu, M., Yang, W., Wang, Z., Phillips, M.J., Levy, G.A. J. Biol. Chem. (2003) [Pubmed]
  7. Antibody responses against SARS coronavirus are correlated with disease outcome of infected individuals. Zhang, L., Zhang, F., Yu, W., He, T., Yu, J., Yi, C.E., Ba, L., Li, W., Farzan, M., Chen, Z., Yuen, K.Y., Ho, D. J. Med. Virol. (2006) [Pubmed]
  8. Baculovirus expression of HCoV-OC43 nucleocapsid protein and development of a Western blot assay for detection of human antibodies against HCoV-OC43. Mourez, T., Vabret, A., Han, Y., Dina, J., Legrand, L., Corbet, S., Freymuth, F. J. Virol. Methods (2007) [Pubmed]
  9. Localization to the nucleolus is a common feature of coronavirus nucleoproteins, and the protein may disrupt host cell division. Wurm, T., Chen, H., Hodgson, T., Britton, P., Brooks, G., Hiscox, J.A. J. Virol. (2001) [Pubmed]
  10. Interaction of the coronavirus nucleoprotein with nucleolar antigens and the host cell. Chen, H., Wurm, T., Britton, P., Brooks, G., Hiscox, J.A. J. Virol. (2002) [Pubmed]
  11. Comprehensive antibody epitope mapping of the nucleocapsid protein of severe acute respiratory syndrome (SARS) coronavirus: insight into the humoral immunity of SARS. Liang, Y., Wan, Y., Qiu, L.W., Zhou, J., Ni, B., Guo, B., Zou, Q., Zou, L., Zhou, W., Jia, Z., Che, X.Y., Wu, Y. Clin. Chem. (2005) [Pubmed]
  12. 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]
  13. Immunogenicity of JHM virus proteins: characterization of a CD4+ T cell epitope on nucleocapsid protein which induces different T-helper cell subsets. van der Veen, R.C. Virology (1996) [Pubmed]
  14. Membrane and phospholipid binding by murine coronaviral nucleocapsid N protein. Anderson, R., Wong, F. Virology (1993) [Pubmed]
  15. Antibody responses to respiratory coronavirus infections of cattle during shipping fever pathogenesis. Lin, X.Q., O eilly, K.L., Storz, J., Purdy, C.W., Loan, R.W. Arch. Virol. (2000) [Pubmed]
  16. Localization of an RNA-binding domain in the nucleocapsid protein of the coronavirus mouse hepatitis virus. Masters, P.S. Arch. Virol. (1992) [Pubmed]
  17. Localization of the RNA-binding domain of mouse hepatitis virus nucleocapsid protein. Nelson, G.W., Stohlman, S.A. J. Gen. Virol. (1993) [Pubmed]
  18. Characterization of the coronavirus M protein and nucleocapsid interaction in infected cells. Narayanan, K., Maeda, A., Maeda, J., Makino, S. J. Virol. (2000) [Pubmed]
  19. Recombinant vaccinia viruses which express MHV-JHM proteins: protective immune response and the influence of vaccination on coronavirus-induced encephalomyelitis. Flory, E., Stühler, A., Wege, H., Siddell, S., Wege, H. Adv. Exp. Med. Biol. (1993) [Pubmed]
  20. Repair and mutagenesis of the genome of a deletion mutant of the coronavirus mouse hepatitis virus by targeted RNA recombination. Koetzner, C.A., Parker, M.M., Ricard, C.S., Sturman, L.S., Masters, P.S. J. Virol. (1992) [Pubmed]
  21. SR-rich motif plays a pivotal role in recombinant SARS coronavirus nucleocapsid protein multimerization. Luo, H., Ye, F., Chen, K., Shen, X., Jiang, H. Biochemistry (2005) [Pubmed]
  22. Location of antibody epitopes within the mouse hepatitis virus nucleocapsid protein. Stohlman, S.A., Bergmann, C., Cua, D., Wege, H., van der Veen, R. Virology (1994) [Pubmed]
  23. Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection. Wesseling, J.G., Godeke, G.J., Schijns, V.E., Prevec, L., Graham, F.L., Horzinek, M.C., Rottier, P.J. J. Gen. Virol. (1993) [Pubmed]
  24. Characterization of a coronavirus isolated from a diarrheic foal. Guy, J.S., Breslin, J.J., Breuhaus, B., Vivrette, S., Smith, L.G. J. Clin. Microbiol. (2000) [Pubmed]
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