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|Title:||Analysis of self-association of West Nile virus capsid protein and the crucial role played by Trp 69 in homodimerization|
|Authors:||Bhuvanakantham, R. |
|Citation:||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|
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