Determinants of dengue virus NS4A protein oligomerization
Xie, Xuping, Zou, Jing, Dong, Hongping and Shi, Pei-Yong (2015) Determinants of dengue virus NS4A protein oligomerization. Journal of Virology, 89 (12). pp. 6171-6183. ISSN 0022-538X
Abstract
We report that dengue virus NS4A protein forms oligomers in infected cells or when expressed alone. Amino acids 50-76, representing the first transmembrane domain (TMD1) of NS4A, constitute the major determinant for oligomerization. Ala-substitution of flavivirus-conserved residues within TMD1 (Glu50 and Gly67) attenuated oligomerization, reduced NS4A protein stability, and impaired viral replication. In contrast, NS4A oligomerization was not affected by replication-defective mutations outside TMD1. The results have demonstrated the importance of TMD1-mediated NS4A oligomerization in dengue virus replication.
Item Type: | Article |
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Date Deposited: | 12 Oct 2016 00:45 |
Last Modified: | 12 Oct 2016 00:45 |
URI: | https://oak.novartis.com/id/eprint/24135 |