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Title: The interdomain region of dengue NS5 protein interacts with NS3 and host proteins.
Authors: Brooks, Andrew J
Johansson, Magnus
Criswell, Erin
Jans, David A
Vasudevan, Subhash G
Issue Date: 2002
Publisher: WHO Regional Office for South-East Asia
Place of publication: New Delhi
Language: English
Abstract: Although dengue virus genome replication occurs in the cytoplasm of infected cells, it has been shown that the NS5 protein (RNA-dependent RNA polymerase) is hyperphosphorylated at a late stage in infection and localized to the cell nucleus. A 37 amino acid sequence of NS5 (residues 369-405)was shown to contain a functional unclear localization signal (NLS) that interacted with the cellular nuclear transport factor, importin α/β heterodimer. Further studies using the yeast two-hybrid system revealed that the NS5 region (residues 320-368) immediately adjacent to the NLS contained an importin β-binding site that abuts or overlaps the binding site for the NS3 protein (protease/helicase). The importin β-binding site has also been shown to be a functional NLS (bNLS). Intriguingly, when both bNLS and NLS (residues 320-405) were present,the fused β -galactosidase protein did not accumulate in the nucleus. Here we provide a review of our studies on the NS5 interdomain region and compare it to other members of the Flavivirus genus in order to highlight the importance of this region as a possible target for developing broad-acting antiviral agent against dengue and other mechanistically-related viruses.
Description: Dengue Bulletin. 2002; 26: 155-161
Keywords: Dengue
RNA Virus
NSS protein
protein interactions
NS3 protein
nuclear localization signal
Appears in Collections:Dengue Bulletin

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