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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 | 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 | URI: | http://scholarbank.nus.edu.sg/handle/10635/31303 | ISSN: | 0006291X | DOI: | 10.1016/j.bbrc.2005.01.121 |
Appears in Collections: | Staff Publications |
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