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Viruses 2015, 7(7), 4119-4130; doi:10.3390/v7072812

Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes

1
Institute of Complex Systems, Structural Biochemistry (ICS-6), Forschungszentrum Jülich,52425 Jülich, Germany
2
Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1,40255 Düsseldorf, Germany
3
Department Clinical Microbiology and Immunology, Sackler School of Medicine,Tel Aviv University, Tel Aviv 69978, Israel
*
Author to whom correspondence should be addressed.
Academic Editor: David Boehr
Received: 30 April 2015 / Revised: 10 July 2015 / Accepted: 13 July 2015 / Published: 21 July 2015
View Full-Text   |   Download PDF [618 KB, uploaded 21 July 2015]   |  

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. View Full-Text
Keywords: Dengue virus (DENV); non-structural protein 4A (NS4A); amphipathic helix; curvature sensing; peptide membrane interaction Dengue virus (DENV); non-structural protein 4A (NS4A); amphipathic helix; curvature sensing; peptide membrane interaction
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Hung, Y.-F.; Schwarten, M.; Hoffmann, S.; Willbold, D.; Sklan, E.H.; Koenig, B.W. Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes. Viruses 2015, 7, 4119-4130.

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