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首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion
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NMR structure and localization of a large fragment of the SARS-CoV fusion protein: Implications in viral cell fusion

机译：SARS-COV融合蛋白的大片段的NMR结构和定位：病毒细胞融合中的影响

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Abstract The lethal Coronaviruses (CoVs), Severe Acute Respiratory Syndrome-associated Coronavirus (SARS-CoV) and most recently Middle East Respiratory Syndrome Coronavirus, (MERS-CoV) are serious human health hazard. A successful viral infection requires fusion between virus and host cells carried out by the surface spike glycoprotein or S protein of CoV. Current models propose that the S2 subunit of S protein assembled into a hexameric helical bundle exposing hydrophobic fusogenic peptides or fusion peptides (FPs) for membrane insertion. The N-terminus of S2 subunit of SARS-CoV reported to be active in cell fusion whereby FPs have been identified. Atomic-resolution structure of FPs derived either in model membranes or in membrane mimic environment would glean insights toward viral cell fusion mechanism. Here, we have solved 3D structure, dynamics and micelle localization of a 64-residue long fusion peptide or LFP in DPC detergent micelles by NMR methods. Micelle bound structure of LFP is elucidated by the presence of discretely folded helical and intervening loops. The C-terminus region, residues F42-Y62, displays a long hydrophobic helix, whereas the N-terminus is defined by a short amphipathic helix, residues R4-Q12. The intervening residues of LFP assume stretches of loops and helical turns. The N-terminal helix is sustained by close aromatic and aliphatic sidechain packing interactions at the non-polar face. 15 N{ 1 H}NOE studies indicated dynamical motion, at ps-ns timescale, of the helices of LFP in DPC micelles. PRE NMR showed that insertion of several regions of LFP into DPC micelle core. Together, the current study provides insights toward fusion mechanism of SARS-CoV. Graphical abstract Display Omitted Highlights ? 3-D structure of long fusion peptide (LFP) of SRAS-CoV in DPC micelles ? LFP adopts helix-loop-helix structure and inserts into micelle. ? The structure provides mechanism of membrane fusion process.
机译：摘要致命冠状病毒（COVS），严重急性呼吸综合征相关的冠状病毒（SARS-COV）和最近中东呼吸综合征冠状病毒（MERS-COV）是严重的人类健康危害。成功的病毒感染需要通过COV的表面尖峰糖蛋白或S蛋白进行的病毒和宿主细胞之间的融合。目前的模型提出，S蛋白的S2亚基组装成曝光疏水性富含肽或融合肽（FPS）的六聚螺旋束进行膜插入。 SARS-COV的S2亚基的N-末端据报道在细胞融合中是活性的，因此已经鉴定了FPS。在模型膜或膜模拟环境中衍生的FPS的原子分辨率结构将对病毒细胞融合机制引起洞察。在这里，通过NMR方法，我们在DPC洗涤剂胶束中解决了3D结构，动力学和胶束定位或在DPC洗涤剂胶束中的LFP。通过离散折叠的螺旋和介入环，阐明LFP的胶束绑定结构。 C-末端区残留物F42-Y62显示出长的疏水螺旋，而N-末端由短的两亲螺旋，残留物R4-Q12定义。 LFP的介入残余物假设延伸环和螺旋匝。 N末端螺旋通过在非极性面上的密切芳香和脂族侧链填充相互作用而持续。 15 N {1 H} NOE研究表明，在PS-NS时间尺度，LFP的LFP螺旋中的动态运动在DPC胶束上。前NMR显示将几个区域的LFP插入DPC胶束芯。在一起，目前的研究为SARS-COV融合机制提供了见解。图形抽象显示省略了亮点？ DPC胶束SRAS-COV长融合肽（LFP）的3-D结构？ LFP采用Helix-Loop-Helix结构并插入胶束中。还该结构提供了膜融合过程的机制。

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