Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms.
Effect of influenza hemagglutinin fusion peptide on lamellar/inverted phase transitions in dipalmitoleoylphosphatidylethanolamine: implications for membrane fusion mechanisms.
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流感血凝素融合肽对二棕榈油酰磷脂酰乙醇胺层状/倒相相变的影响:对膜融合机制的影响。
DOI:
10.1016/s0005-2736(00)00246-7
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发表时间:
2000
期刊:
影响因子:
--
通讯作者:
Epand,RM
中科院分区:
文献类型:
--
作者:
Siegel,DP;Epand,RM
Low mole fractions of viral fusion peptides induce inverted cubic (QII) phases in dipalmitoleoylphosphatidylethanolamine (DiPoPE), a lipid with unsaturated acyl chains that normally forms inverted hexagonal phase (HII) above 43°C. The ability to form a QIIphase is relevant to the study of membrane fusion: fusion occurs in liposomal systems under conditions where QIIphase precursors form, and fusion may be an obligatory step in the lamellar (Lα)/QIIphase transition. We used X-ray diffraction and time-resolved cryoelectron microscopy (TRC-TEM) to study the effects of the influenza hemagglutinin fusion peptide on the phase behavior and structure of DiPoPE. X-ray diffraction data show that at concentrations of 3–7 mol%, the fusion peptide (FP) induces formation of a QIIphase in preference to the HIIphase. TRC-TEM data show that the FP acts at early stages in the phase transition (i.e. within seconds): at 2–7 mol%, FP decreases or inhibits formation of the Lα/HIIintermediate morphology observed via TRC-TEM in pure DiPoPE at the same temperature. Our X-ray diffraction data imply that FP either does not affect, or slightly increases, the spontaneous curvature of the host lipid (i.e. either does not affect or tends to destabilize inverted phases, respectively). FP may act in part by affecting the relative stability of two intermediate structures in the phase transition mechanism, as suggested previously. These results indicate a new way in which hydrophobic sequences of membrane proteins may be fusogenic.
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影响因子:
3.4
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