TY  - JOUR
AU  - Hung, Yu-Fu
AU  - Schwarten, Melanie
AU  - Hoffmann, Silke
AU  - Willbold, Dieter
AU  - Sklan, Ella
AU  - König, Bernd
TI  - Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes
JO  - Viruses
VL  - 7
IS  - 7
SN  - 1999-4915
CY  - Basel
PB  - MDPI
M1  - FZJ-2015-06971
SP  - 4119 - 4130
PY  - 2015
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000360353200038
C6  - pmid:26197333
DO  - DOI:10.3390/v7072812
UR  - https://juser.fz-juelich.de/record/276643
ER  -