scholarly journals Synthesis of Bluetongue Virus Chimeric VP3 Molecules and Their Interactions with VP7 Protein to Assemble into Virus Core-like Particles

Virology ◽  
1995 ◽  
Vol 214 (2) ◽  
pp. 593-601 ◽  
Author(s):  
SEIICHI TANAKA ◽  
MICHAEL MIKHAILOV ◽  
POLLY ROY
Keyword(s):  
Bluetongue Virus ◽  
Virus Core ◽  
Vp7 Protein

A multi-species indirect ELISA for detection group-specific antibodies against VP7 protein of bluetongue virus

2019 ◽  
Vol 180 ◽  
pp. 6-8 ◽  
Author(s):  
Karam Chand ◽  
Sanchay Kumar Biswas ◽  
Muthannan Andavar Ramakrishnan
Keyword(s):  
Bluetongue Virus ◽  
Indirect Elisa ◽  
Specific Antibodies ◽  
Vp7 Protein

scholarly journals In Silico Studies on Development of Novel Virostatic Agents against Bluetongue Virus

ISRN Virology ◽  
2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Pandrangi Anupama
Keyword(s):  
Bluetongue Virus ◽  
Core Protein ◽  
Critical Role ◽  
Docking Studies ◽  
Site Specific ◽  
The Core ◽  
In Silico Studies ◽  
Vp7 Protein ◽  
Major Core Protein

The core of BTV is organized into three concentric structures of which VP7 protein forms the major core protein. The subcore consists of VP3 protein and the innermost part of the core is made of three minor proteins: VP1, VP4, and VP6. Earlier it was reported that core-like particles (CLPs) composed of viral VP7 and VP3 proteins were produced in order to study role of VP7 protein in intermolecular interactions in the BTV assembly process. Site specific mutational studies revealed that substitution of the single lysine residue of VP7 (Lys-255) by leucine abrogated CLP formation, indicating a critical role for this lysine. In the present study, homology modeling, mutagenesis, and docking studies were carried out in order to design potent leads in modulation of VP7 protein in abrogating CLP formation.

Vaccinia virus expression of the VP7 protein of South African bluetongue virus serotype 4 and its use as an antigen in a capture ELISA

1994 ◽  
Vol 135 (3-4) ◽  
pp. 405-418 ◽  
Author(s):  
M. Cloete ◽  
D. H. du Plessis ◽  
A. A. van Dijk ◽  
H. Huismans ◽  
G. J. Viljoen
Keyword(s):  
Vaccinia Virus ◽  
South African ◽  
Bluetongue Virus ◽  
Capture Elisa ◽  
Virus Serotype ◽  
Vp7 Protein ◽  
Virus Expression

scholarly journals Intermolecular Interactions in a Two-Layered Viral Capsid That Requires a Complex Symmetry Mismatch

2003 ◽  
Vol 77 (20) ◽  
pp. 11114-11124 ◽  
Author(s):  
Chang-Kwang Limn ◽  
Polly Roy
Keyword(s):  
Virus Assembly ◽  
Single Gene ◽  
Complex Structure ◽  
Sequence Information ◽  
Multiple Site ◽  
Virus Core ◽  
Vp7 Protein ◽  
Trimer Formation ◽  
Substitution Mutations ◽  
Protein Shell

ABSTRACT The surface of the bluetongue virus core forms a T=13 quasiequivalent icosahedral protein shell with 260 trimers of a single gene product: VP7 protein. Underneath is a smooth layer, made up of VP3 protein, which appears to guide and nucleate the assembly of VP7 trimers. The contacts between the two shells are extensive but nonspecific, and construction of the T=13 icosahedral shell requires polymorphism in the association of the VP7 subunits, each of which has two domains that contribute to trimer formation. We used structural and relative sequence information to guide an investigation of how such a complex structure is achieved during virus assembly and what residues are required to form a stable capsid. Fifteen single or multiple site-specific substitution mutations were introduced into the helical domain of VP7, which is closely associated with the VP3 layer, and the effects on capsid assembly were analyzed. Our data show that both the position and the nature of single residues are critical for the attachment of VP7 to VP3 and that formation of a stable VP7 lattice is not the automatic consequence of trimer formation.

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