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- Title
Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes.
- Authors
Yu-Fu Hung; Koenig, Bernd W.; Schwarten, Melanie; Sklan, Ella H.; Willbold, Dieter; Hoffmann, Silke
- Abstract
Dengue virus (DENV) is an important human pathogen causing millions of disease cases and thousands of deaths worldwide. Non-structural protein 4A (NS4A) is a vital component of the viral replication complex (RC) and plays a major role in the formation of host cell membrane-derived structures that provide a scaffold for replication. The N-terminal cytoplasmic region of NS4A(1-48) is known to preferentially interact with highly curved membranes. Here, we provide experimental evidence for the stable binding of NS4A(1-48) to small liposomes using a liposome floatation assay and identify the lipid binding sequence by NMR spectroscopy. Mutations L6E;M10E were previously shown to inhibit DENV replication and to interfere with the binding of NS4A(1-48) to small liposomes. Our results provide new details on the interaction of the N-terminal region of NS4A with membranes and will prompt studies of the functional relevance of the curvature sensitive membrane anchor at the N-terminus of NS4A.
- Subjects
DENGUE viruses; VIRAL nonstructural proteins; VIRAL replication; ALPHA helix structure (Proteins); CURVATURE; PEPTIDES; LIPOSOMES; NUCLEAR magnetic resonance spectroscopy
- Publication
Viruses (1999-4915), 2015, Vol 7, Issue 7, p4119
- ISSN
1999-4915
- Publication type
Article
- DOI
10.3390/v7072812