An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication

Omer Stern; Yu Fu Hung; Olga Valdau; Yakey Yaffe; Eva Harris; Silke Hoffmann; Dieter Willbold; Ella H. Sklan

doi:10.1128/JVI.01900-12

An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication

Omer Stern, Yu Fu Hung, Olga Valdau, Yakey Yaffe, Eva Harris, Silke Hoffmann, Dieter Willbold, Ella H. Sklan^*

^*Corresponding author for this work

Clinical Microbiology and Immunology

Research output: Contribution to journal › Article › peer-review

59 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	4080-4085
Number of pages	6
Journal	Journal of Virology
Volume	87
Issue number	7
DOIs	https://doi.org/10.1128/JVI.01900-12
State	Published - Apr 2013

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10.1128/JVI.01900-12

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abstract = "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.",

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AU - Hung, Yu Fu

AU - Valdau, Olga

AU - Yaffe, Yakey

AU - Harris, Eva

AU - Hoffmann, Silke

AU - Willbold, Dieter

AU - Sklan, Ella H.

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An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication

Abstract

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