杆状病毒蛋白融合肽LdF在溶液中的NMR结构研究

NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein

LD130是舞毒蛾核多角体病毒(Lymantria dispar multiple nucleopolyhedrovirus,LdMNPV)的膜融合蛋白(F蛋白),其F1亚基N端疏水的保守区为介导膜融合过程的活性肽段,即融合肽区域.利用核磁共振的方法,确定了该融合肽在酸性条件下类膜环境中的溶液结构.结果表明融合肽LdF具有典型的α螺旋结构,整个肽段于类膜环境中呈现两亲性,即螺旋沿轴向可分为亲水侧面和亲脂侧面.该结构有利于对病毒囊膜与细胞膜融合过程的深入理解与研究.

LD130 is the fusion protein of baculoviruse Lymantria dispar multiple nucle-opolyhedrovirus （LdMNPV）. The N terminal conserved region of subunit F1 in LD130 is the fusion peptide, which actively induces membrane fusion processes. NMR methods were used to identify the solution structure of the fusion peptide under membrane simu- lated enviornment at low pH. The fusion peptide appeared to be an amphiphilie structure composed of a flexible coil in the N-terminus, and a regular a-helix from L3 to V16. The structure of the LD130 fusion peptide allows us to further investigate the structure-functional relationship of the fusion peptide.