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The Nucleocapsid Protein of Coronavirus Infectious Bronchitis Virus: Crystal Structure of Its N-Terminal Domain and Multimerization Properties

Authors :
Fan, Hui
Ooi, Amy
Tan, Yong Wah
Wang, Sifang
Fang, Shouguo
Liu, Ding Xiang
Lescar, Julien
Source :
Structure. Dec2005, Vol. 13 Issue 12, p1859-1868. 10p.
Publication Year :
2005

Abstract

Summary: The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29–160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 Å resolution reveals a protein core composed of a five-stranded antiparallel β sheet with a positively charged β hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
09692126
Volume :
13
Issue :
12
Database :
Academic Search Index
Journal :
Structure
Publication Type :
Academic Journal
Accession number :
19183852
Full Text :
https://doi.org/10.1016/j.str.2005.08.021