%0 Journal Article
%A Hung, Yu-Fu
%A Schwarten, Melanie
%A Hoffmann, Silke
%A Willbold, Dieter
%A Sklan, Ella
%A König, Bernd
%T Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes
%J Viruses
%V 7
%N 7
%@ 1999-4915
%C Basel
%I MDPI
%M FZJ-2015-06971
%P 4119 - 4130
%D 2015
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000360353200038
%$ pmid:26197333
%R 10.3390/v7072812
%U https://juser.fz-juelich.de/record/276643