title: An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.
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.
authors: Department of Clinical Microbiology and Immunology, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel.
authors: Omer
authors: O
authors: Stern
authors: Yu-Fu
authors: YF
authors: Hung
authors: Olga
authors: O
authors: Valdau
authors: Yakey
authors: Y
authors: Yaffe
authors: Eva
authors: E
authors: Harris
authors: Silke
authors: S
authors: Hoffmann
authors: Dieter
authors: D
authors: Willbold
authors: Ella H
authors: EH
authors: Sklan
mesh_terms: D000595:Amino Acid Sequence; D015153:Blotting, Western; D003716:Dengue Virus / Q000235:genetics*; D040461:Gene Components; D018613:Microscopy, Confocal; D008969:Molecular Sequence Data; D016296:Mutagenesis; D058105:Polymerization; D016415:Sequence Alignment; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000378:metabolism; D014779:Virus Replication / Q000235:genetics*
chemical_list: D017361:Viral Nonstructural Proteins