Recombinant Human SARS coronavirus Nucleoprotein (N)

1. The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. PMID: 28148787
2. Electrostatic repulsion acts as a switch to regulate SARS virus N protein oligomerization. PMID: 23717688
3. These results suggest that SARS coronavirus could reduce pyruvate kinase activity via its nucleocapsid protein, and this may in turn cause disease. PMID: 22222284
4. The co-localization of SARS-CoVN and CXCL16 in the cytoplasm of HEK293FT cells was also shown using confocal laser scanning microscopy. PMID: 20960183
5. The HLA-A 2402 complexed with SARSV N1 showed a novel host strategy to present an immunodominant CTL epitope by intrachain hydrogen bond as a featured epitope. PMID: 20844028
6. SARS-CoV N interacts with MAP19 and increased the expression of MAP19 in cells. PMID: 19737459
7. This is the first report showing the ability of the nucleocapsid protein of SARS-CoV to induce apoptosis and actin reorganization in mammalian cells under stressed conditions. PMID: 15294014
8. analysis of SARS-CoV nucleocapsid protein expressed in insect cells PMID: 15514849
9. The nucleocapsid protein of the SARS coronavirus was cloned and purified. PMID: 15523835
10. Binding to cyclophilin A during invasion of host cells. PMID: 15688292
11. coronavirus N protein undergoes posttranslational modification by sumoylation; functional implication of this modification in the formation of coronavirus ribouncleoprotein complex, virion assembly and virus-host interactions PMID: 15848177
12. the nucleocapsid protein forms a dimer through its C-terminal domain PMID: 15849181
13. Differences in nuclear/nucleolar localization properties of N from other members of coronavirus family suggest a unique shuttle protein function for N, which may play an important role in the pathogenesis of SARS. PMID: 15992957
14. results showed that the SARS-CoV N protein can significantly activate NF-kappaB only in Vero E6 cells, which are susceptible to SARS-CoV infection, but not in Vero or HeLa cells; suggests that NF-kappaB activation is cell-specific PMID: 16143815
15. The secondary structure of the dimerization domain consists of five alpha helices and a beta-hairpin. PMID: 16214138
16. Results show that the N protein consists of two non-interacting structural domains, the N-terminal RNA-binding domain (RBD) (residues 45-181) and the C-terminal dimerization domain (residues 248-365) (DD), surrounded by flexible linkers. PMID: 16228284
17. data suggest that the SR-rich motif of the SARS-CoV N protein might play an import role in the transformation of the SARS-CoV N protein between the dimer and multimer during its binding to its central region for self-association or dissociation PMID: 16285739
18. cytoplasmic localization was directed by region III and was the dominant localization signal in the N protein. PMID: 16298975
19. the S phase inhibitory activity of the N protein may have major significance during viral pathogenesis PMID: 16431923
20. the N protein has a dimer with extensive interactions between the two subunits, suggesting that the dimeric form of the N protein is the functional unit in vivo PMID: 16627473
21. using the solution structure of severe acute respiratory (SARS) coronavirus N-protein, revealed that this motif is available for interaction with cellular factors which may mediate nucleolar localization PMID: 16734668
22. This is the first report demonstrating the interaction of hUbc9 with a structural protein of plus-strand RNA viruses, indicating a new drug target for SARS-CoV. PMID: 16998888
23. the nucleocapsid protein of severe acute respiratory syndrome coronavirus is sumoylated by interaction with Ubc9 PMID: 17037517
24. characterization of the structures of N protein N-terminal domain in two crystal forms, at 1.17 A (monoclinic) and at 1.85 A (cubic), respectively PMID: 17229691
25. The C-terminal domain (CTD), spanning residues 248-365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. The crystal structure of the NP248-365 region is solved, suggesting a mechanism for helical RNA packaging in the virus. PMID: 17379242
26. SARS coronavirus N protein can induce apoptosis of COS-1 cells by activating mitochondrial pathway PMID: 17453707
27. We also showed that N protein activated IL-6 expression through NF-kappaB by facilitating the translocation of NF-kappaB from cytosol to nucleus. PMID: 17490702
28. SARS coronavirus nucleocapsid protein interacts with Smad3 and modulates transforming growth factor-beta signaling PMID: 18055455
29. The experiments revealed that N induces the intrinsic apoptotic pathway, resulting in processing of N at residues 400 and 403 by caspase-6 and/or caspase-3. PMID: 18155731
30. fgl2 gene transcription induced by the N protein of SARS-CoV was dependent on transcription factor C/EBP alpha binding with its cognate cis-element in fgl2 promoter. PMID: 18390877
31. It was demonstrated that the N protein of SARS-CoV induces aggregation of EF1, inhibiting protein translation and cytokinesis by blocking F-actin bundling. PMID: 18448518
32. This study employed the SAIL method to determine the high-quality solution structure of the severe acute respiratory syndrome coronavirus nucleocapsid protein C-terminal domain by NMR. PMID: 18561946
33. the domain conferring the ability to direct virus-like particle assembly and release in SARS-CoV N is largely contained between residues 168 and 421 PMID: 18592403
34. Phosphorylation of the arginine/serine motif of the nucleocapsid protein did not significantly affect RNA binding of the nucleocapsid protein but impaired its multimerization ability. PMID: 18631359
35. This paper describes the work to identify two proteins/protein fragments of N protein and to determine their source. PMID: 18926799
36. An excessive host immune response against the nucleocapsid protein of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is involved in severe pneumonia caused by SARS-CoV infection. PMID: 18941225
37. The SARS-CoV N protein is a modular protein containing multiple RNA-binding sites. PMID: 19052082
38. thermostability of the N-terminal RNA-binding domain (RBD) of the N protein; results showed the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90% PMID: 19254548
39. SR-rich motif is critical for effective virus replication. PMID: 19370068
40. SARS-CoV N protein specifically modulates transcription of the FGL2 gene to cause fibrosis and vascular thrombosis. PMID: 19423547

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KEGG: vg:1489678