Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy

Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy
Title:
Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy
Other Titles:
Biochimica et Biophysica Acta - Biomembranes
Publication Date:
11 June 2015
Citation:
Yan Li, Qingxin Li, Ying Lei Wong, Lynette Sin Yee Liew, CongBao Kang, Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy, Biochimica et Biophysica Acta (BBA) - Biomembranes, Available online 11 June 2015, ISSN 0005-2736, http://dx.doi.org/10.1016/j.bbamem.2015.06.010. (http://www.sciencedirect.com/science/article/pii/S000527361500190X)
Abstract:
Non-structural (NS) proteins of dengue virus (DENV) are important for viral replication. There are four membrane proteins that are coded by viral genome. NS2B was shown to be one of the membrane proteins and its main function was confirmed to regulate viral protease activity. Its membrane topology is still not known because only few studies have been conducted to understand its structure. Here we report the determination of membrane topology of NS2B from DENV serotype 4 using NMR spectroscopy. NS2B of DENV4 was expressed and purified in detergent micelles. The secondary structure of NS2B was first defined based on backbone chemical resonance assignment. Four helices were identified in NS2B. The membrane topology of NS2B was defined based on relaxation analysis and paramagnetic relaxation enhancement experiments. The last three helices were shown to be more stable than the first helices. The NS3 protease cofactor region between α2 and α3 is highly dynamic. Our results will be useful for further structural and functional analysis of NS2B.
License type:
http://creativecommons.org/licenses/by-nc-nd/4.0/
Funding Info:
A*STAR JCO grants (1331A028 and 1231B015).
Description:
ISSN:
0006-3002
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