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@ARTICLE{Hung:276643,
author = {Hung, Yu-Fu and Schwarten, Melanie and Hoffmann, Silke and
Willbold, Dieter and Sklan, Ella and König, Bernd},
title = {{A}mino {T}erminal {R}egion of {D}engue {V}irus {NS}4{A}
{C}ytosolic {D}omain {B}inds to {H}ighly {C}urved
{L}iposomes},
journal = {Viruses},
volume = {7},
number = {7},
issn = {1999-4915},
address = {Basel},
publisher = {MDPI},
reportid = {FZJ-2015-06971},
pages = {4119 - 4130},
year = {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.},
cin = {ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {553 - Physical Basis of Diseases (POF3-553)},
pid = {G:(DE-HGF)POF3-553},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000360353200038},
pubmed = {pmid:26197333},
doi = {10.3390/v7072812},
url = {https://juser.fz-juelich.de/record/276643},
}