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000203112 1001_ $$0P:(DE-Juel1)140558$$aHung, Yu-Fu$$b0
000203112 245__ $$aDengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature
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000203112 520__ $$aDengue virus (DENV) infection is a growing public health threat with more than one-third of the world's population at risk. Non-structural protein 4A (NS4A), one of the least characterized viral proteins, is a highly hydrophobic transmembrane protein thought to induce the membrane alterations that harbor the viral replication complex. The NS4A N-terminal (amino acids 1–48), has been proposed to contain an amphipathic α-helix (AH). Mutations (L6E; M10E) designed to reduce the amphipathic character of the predicted AH, abolished viral replication and reduced NS4A oligomerization. Nuclear magnetic resonance (NMR) spectroscopy was used to characterize the N-terminal cytoplasmic region (amino acids 1–48) of both wild type and mutant NS4A in the presence of SDS micelles. Binding of the two N-terminal NS4A peptides to liposomes was studied as a function of membrane curvature and lipid composition. The NS4A N-terminal was found to contain two AHs separated by a non-helical linker. The abovementioned mutations did not significantly affect the helical secondary structure of this domain. However, they reduced the affinity of the N-terminal NS4A domain for lipid membranes. Binding of wild type NS4A(1–48) to liposomes is highly dependent on membrane curvature.
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000203112 7001_ $$0P:(DE-Juel1)132019$$aSchwarten, Melanie$$b1
000203112 7001_ $$0P:(DE-Juel1)132020$$aSchünke, Sven$$b2
000203112 7001_ $$0P:(DE-HGF)0$$aThiagarajan-Rosenkranz, Pallavi$$b3
000203112 7001_ $$0P:(DE-Juel1)132003$$aHoffmann, Silke$$b4
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000203112 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b6
000203112 7001_ $$0P:(DE-Juel1)132009$$aKönig, Bernd$$b7$$eCorresponding author$$ufzj
000203112 773__ $$0PERI:(DE-600)2209384-9$$a10.1016/j.bbamem.2015.01.015$$gVol. 1848, no. 5, p. 1119 - 1126$$n5$$p1119 - 1126$$tBiochimica et biophysica acta / Biomembranes$$v1848$$x0005-2736$$y2015
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