Please use this identifier to cite or link to this item:
|Title:||Analysis of self-association of West Nile virus capsid protein and the crucial role played by Trp 69 in homodimerization|
|Authors:||Bhuvanakantham, R. |
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 6, 2017
WEB OF SCIENCETM
checked on Nov 22, 2017
checked on Dec 10, 2017
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.