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首页> 外文期刊>Biochemistry >Pressure-induced fusogenic conformation of vesicular stomatitis virus glycoprotein.
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Pressure-induced fusogenic conformation of vesicular stomatitis virus glycoprotein.

机译：压力诱导的水泡性口腔炎病毒糖蛋白融合构象。

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摘要

Vesicular stomatitis virus (VSV) is composed of a ribonucleoprotein core surrounded by a lipid envelope presenting an integral glycoprotein (G). The homotrimeric VSV G protein exhibits a membrane fusion activity that can be elicited by low pH. The fusion event is crucial to entry into the cell and disassembly followed by viral replication. To understand the conformational changes involved in this process, the effects of high hydrostatic pressure and urea on VSV particles and isolated G protein were investigated. With pressures up to 3.0 kbar VSV particles were converted into the fusogenic conformation, as measured by a fusion assay and by the binding of bis-ANS. The magnitude of the changes was similar to that promoted by lowering the pH. To further understand the relationship between stability and conversion into the fusion-active states, the stability of the G protein was tested against urea and high pressure. High urea produced a large red shift in the tryptophan fluorescence of G protein whereas pressure promoted a smaller change. Pressure induced equal fluorescence changes in isolated G protein and virions, indicating that virus inactivation induced by pressure is due to changes in the G protein. Fluorescence microscopy showed that pressurized particles were capable of fusing with the cell membrane without causing infection. We propose that pressure elicits a conformational change in the G protein, which maintains the fusion properties but suppresses the entry of the virus by endocytosis. Binding of bis-ANS indicates the presence of hydrophobic cavities in the G protein. Pressure also caused an increase in light scattering of VSV G protein, reinforcing the hypothesis that high pressure elicits the fusogenic activity of VSV G protein. This "fusion-intermediate state" induced by pressure has minor changes in secondary structure and is likely the cause of nonproductive infections.
机译：水泡性口炎病毒（VSV）由核糖核蛋白核心组成，核糖核蛋白核心周围包裹着呈完整糖蛋白（G）的脂质包膜。同型三聚体VSV G蛋白表现出膜融合活性，这可由低pH引起。融合事件对于进入细胞并在随后的病毒复制中解体至关重要。为了了解此过程涉及的构象变化，研究了高静水压力和尿素对VSV颗粒和分离的G蛋白的影响。在高达3.0 kbar的压力下，通过融合测定和bis-ANS的结合测量，VSV颗粒转变为融合构象。变化的幅度与降低pH值所促进的变化相似。为了进一步了解稳定性与转化为融合活性状态之间的关系，测试了G蛋白对尿素和高压的稳定性。高尿素会在G蛋白的色氨酸荧光中产生较大的红移，而压力则促进较小的变化。压力诱导分离的G蛋白和病毒体中荧光变化相等，这表明压力诱导的病毒灭活是由于G蛋白的变化所致。荧光显微镜显示加压颗粒能够与细胞膜融合而不会引起感染。我们提出，压力会引起G蛋白的构象变化，从而保持融合特性，但通过内吞作用抑制病毒的进入。 bis-ANS的结合表明G蛋白中存在疏水腔。压力还导致VSV G蛋白的光散射增加，从而增强了高压引发VSV G蛋白融合活性的假说。由压力引起的这种“融合-中间状态”在二级结构上有微小变化，很可能是非生产性感染的原因。

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