Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2004.03.154
Title: The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain
Authors: Surjit, M.
Kumar, P.
Lal, S.K.
Liu, B. 
Chow, V.T.K. 
Keywords: Nucleocapsid protein
Protein-protein interaction
SARS coronavirus
Yeast two-hybrid system
Issue Date: 2004
Source: Surjit, M., Kumar, P., Lal, S.K., Liu, B., Chow, V.T.K. (2004). The nucleocapsid protein of the SARS coronavirus is capable of self-association through a C-terminal 209 amino acid interaction domain. Biochemical and Biophysical Research Communications 317 (4) : 1030-1036. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2004.03.154
Abstract: Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) caused a severe outbreak in several regions of the world in 2003. The virus is a novel coronavirus isolated from patients exhibiting atypical pneumonia and may have originated from wild animals such as civet cats in southern China. The genome of SARS-CoV is a positive-sense, single-stranded RNA whose sequence is distantly related to all known coronaviruses that infect humans and animals. Like other known coronaviruses, SARS-CoV is an enveloped virus containing three outer structural proteins, namely the membrane (M), envelope (E), and spike (S) proteins. The nucleocapsid (N) protein together with the viral RNA genome presumably form a helical core located within the viral envelope. The SARS-CoV nucleocapsid (N) protein is a 423 amino-acid, predicted phospho-protein of 46kDa that shares little homology with other members of the coronavirus family. A short serine-rich stretch, and a putative bipartite nuclear localization signal are unique to it, thus suggesting its involvement in many important functions during the viral life cycle. In this report we have cloned the N gene of the SARS coronavirus, and studied its property of self-association to form dimers. We expressed the N protein as a fusion protein in the yeast two-hybrid system to demonstrate self-association and confirmed dimerization of the N protein from mammalian cell lysates by coimmunoprecipitation. Furthermore, via deletion analysis, we have shown that the C-terminal 209 amino-acid region constitutes the interaction domain responsible for self-association of the N protein to form dimers. © 2004 Elsevier Inc. All rights reserved.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/31286
ISSN: 0006291X
DOI: 10.1016/j.bbrc.2004.03.154
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

71
checked on Dec 18, 2017

WEB OF SCIENCETM
Citations

62
checked on Nov 21, 2017

Page view(s)

128
checked on Dec 17, 2017

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.