融合肽下方的侧链包装强烈调节亨德拉病毒 F 蛋白的触发。
Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F protein.
机构信息
Department of Molecular and Cellular Biochemistry, University of Kentucky, College of Medicine, Biomedical Biological Sciences Research Building, 741 South Limestone, Lexington, KY 40536-0509, USA.
出版信息
J Virol. 2010 Oct;84(20):10928-32. doi: 10.1128/JVI.01108-10. Epub 2010 Aug 11.
Abstract
Triggering of the Hendra virus fusion (F) protein is required to initiate the conformational changes which drive membrane fusion, but the factors which control triggering remain poorly understood. Mutation of a histidine predicted to lie near the fusion peptide to alanine greatly reduced fusion despite wild-type cell surface expression levels, while asparagine substitution resulted in a moderate restoration in fusion levels. Slowed kinetics of six-helix bundle formation, as judged by sensitivity to heptad repeat B-derived peptides, was observed for all H372 mutants. These data suggest that side chain packing beneath the fusion peptide is an important regulator of Hendra virus F triggering.
摘要
触发亨德拉病毒融合（F）蛋白是启动构象变化从而驱动膜融合所必需的，但是控制触发的因素仍知之甚少。将预测位于融合肽附近的组氨酸突变为丙氨酸，尽管野生型细胞表面表达水平正常，但大大降低了融合效率，而天冬酰胺取代则导致融合水平适度恢复。通过对七肽重复 B 衍生肽的敏感性判断，所有 H372 突变体的六螺旋束形成动力学都明显减慢。这些数据表明，融合肽下方的侧链堆积是亨德拉病毒 F 触发的重要调节剂。
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