Lokesh, GL and Gowri, TDS and Satheshkumar, PS and Murthy, MRN and Savithri, HS (2002) A Molecular Switch in the Capsid Protein Controls the Particle Polymorphism in an Icosahedral Virus. In: Virology, 292 (2). pp. 211-223.
Restricted to Registered users only
Download (1222Kb) | Request a copy
The recombinant coat protein (CP) of Sesbania mosaic virus (SeMV; genus Sobemovirus) was found to self-assemble into capsids encapsidating 23S rRNA and CP mRNA in Escherichia coli. The CP lacking 22 amino acids from the N-terminus assembled into stable T = 3 capsids that appeared similar to SeMV, indicating that the N-terminal 22 amino acid residues are dispensable for T = 3 assembly. Two distinct capsids, T = 1 and pseudo T = 2, were observed when the N-terminal 36 amino acids encompassing the arginine-rich motif (N-ARM) were removed. Only T = 1 particles were observed upon deletion of 65 amino acids from the N-terminus, which also included the sequence element for the β-annulus. These results reveal that N-ARM acts as a molecular switch in regulating T = 3 assembly. Formation of stable pseudo T = 2 particles shows that pentamers of AB dimers could nucleate assembly at icosahedral-5-folds. Capsids assembled from the N-terminally truncated proteins also encapsidated 23S rRNA and CP mRNA, suggesting the presence of sites outside the N-terminal 65 residues that may be involved in RNA–protein interactions.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Elsevier.|
|Keywords:||Icosahedral virus;Virus assembly;Coat protein;Sobemovirus;Sesbania mosaic virus|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Biochemistry
|Date Deposited:||09 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
Actions (login required)