Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbrc.2005.01.121
Title: Analysis of self-association of West Nile virus capsid protein and the crucial role played by Trp 69 in homodimerization
Authors: Bhuvanakantham, R. 
Ng, M.-L. 
Keywords: Capsid
Co-immunoprecipitation
Homotypic interaction
Mammalian two-hybrid
Tryptophan
Yeast two-hybrid
Issue Date: 2005
Source: Bhuvanakantham, R., Ng, M.-L. (2005). Analysis of self-association of West Nile virus capsid protein and the crucial role played by Trp 69 in homodimerization. Biochemical and Biophysical Research Communications 329 (1) : 246-255. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbrc.2005.01.121
Abstract: The understanding of capsid (C) protein interactions with itself would provide important data on how the core is organized in flaviviruses during assembly. In this study, West Nile (WN) virus C protein was shown to form homodimers using yeast two-hybrid analysis in conjunction with mammalian two-hybrid and in vivo co-immunoprecipitation assays. To delineate the region on the C protein which mediates C-C dimerization, truncation studies were carried out. The results obtained clearly showed that the internal hydrophobic segment flanked by helix I and helix III of WN virus C protein is essential for the self-association of C protein. The crucial role played by Trp 69 in stabilizing the self-association of C protein was also demonstrated by mutating Trp to Gly/Arg/Phe. Substitution of the Trp residue with Gly/Arg abolished the dimerization, whereas substitution with Phe decreased the self-association significantly. The results of this study pinpoint a critical residue in the C protein that potentially plays a role in stabilizing the homotypic interaction. © 2005 Elsevier Inc. All rights reserved.
Source Title: Biochemical and Biophysical Research Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/31303
ISSN: 0006291X
DOI: 10.1016/j.bbrc.2005.01.121
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