This title appears in the Scientific Report :
2013
Please use the identifier:
http://dx.doi.org/10.1128/JVI.01900-12 in citations.
An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.
An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.
Dengue virus (DENV) causes dengue fever, a major health concern worldwide. We identified an amphipathic helix (AH) in the N-terminal region of the viral nonstructural protein 4A (NS4A). Disruption of its amphipathic nature using mutagenesis reduced homo-oligomerization and abolished viral replicatio...
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Personal Name(s): | Stern,O. (Corresponding author) |
---|---|
Hung, Yu-Fu / Valdau, Olga / Yaffe,Y. / Harris,E. / Hoffmann, Silke / Willbold, Dieter / Sklan,E. | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Journal of virology, 87 7, S. 4080-4085 |
Imprint: |
Baltimore, Md.
Soc.
2013
|
DOI: |
10.1128/JVI.01900-12 |
Document Type: |
Journal Article |
Research Program: |
Signalling Pathways and Mechanisms in the Nervous System Structural Biology |
Publikationsportal JuSER |
Dengue virus (DENV) causes dengue fever, a major health concern worldwide. We identified an amphipathic helix (AH) in the N-terminal region of the viral nonstructural protein 4A (NS4A). Disruption of its amphipathic nature using mutagenesis reduced homo-oligomerization and abolished viral replication. These data emphasize the significance of NS4A in the life cycle of the dengue virus and demarcate it as a target for the design of novel antiviral therapy. |