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Molecular modeling and conformational analysis of native and refolded viral genome-linked protein of Cardamom mosaic virus

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Title Molecular modeling and conformational analysis of native and refolded viral genome-linked protein of Cardamom mosaic virus
 
Creator Jebasingh, T
Jose, M
Yadunandam, A Kasin
Backiyarani, S
Srividhya, K V
Krishnaswamy, S
Usha, R
 
Subject Viral genome-linked protein
Cardamom mosaic virus
Potyvirus
Inclusion bodies
 
Description 336-340
The viral genome-linked protein (VPg) of
Potyviruses is covalently attached to the 5’ end of the genomic RNA. Towards biophysical
characterization, the VPg coding region of
Cardamom mosaic virus (CdMV) was amplified from the cDNA and expressed in E. coli. Most of the expressed VPg aggregated as inclusion bodies that were
solubilized with urea and refolded with L-arginine hydrochloride. The various
forms of CdMV VPg (native, denatured and refolded) were
purified and the conformational variations between these forms were observed
with fluorescence spectroscopy. Native and refolded CdMV VPg showed unordered
secondary structure in the circular dichroism (CD) spectrum. The model of CdMV
VPg was built based on the crystal structure of phosphotriesterase (from Pseudomonas
diminuta), which had the
maximum sequence homology with VPg to
identify the arrangement of conserved amino acids in the protein to study the
functional diversity of VPg. This is the first report on the VPg of
CdMV, which is classified as a new member of the Macluravirus genus of the
Potyviridae family.
 
Date 2011-10-21T11:02:57Z
2011-10-21T11:02:57Z
2011-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/12942
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.48(5) [October 2011]