杆状病毒HaF融合肽在中性pH溶液中的NMR结构研究

波谱学杂志

杆状病毒HaF融合肽在中性pH溶液中的NMR结构研究

曾丹云^1,2，杜天鹏^1,2，姜凌^1*，刘买利¹

1. 波谱与原子分子物理国家重点实验室，武汉磁共振中心(中国科学院武汉物理与数学研究所)，湖北武汉 430071； 
2. 中国科学院大学，北京 100049

收稿日期:2012-07-23 修回日期:2012-08-28 出版日期:2013-06-05 发布日期:2013-06-05
作者简介:曾丹云（1984-），女，湖北人，博士研究生，从事蛋白溶液结构的核磁共振研究. *通讯联系人：姜凌，电话：027-87198493，E-mail: lingjiang@wipm.ac.cn.
基金资助:
国家自然科学基金资助项目（21173257，20921004）.

NMR Structure of Fusion Peptide of the Helicoverpa Armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein at pH 7.0

ZENG Dan-yun^1,2, DU Tian-peng^1,2, JIANG Ling^1*, LIU Mai-li¹

1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center of Magnetic Resonance (Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences), Wuhan 430071, China;
2. University of Chinese Academy of Sciences, Beijing 100049, China

Received:2012-07-23 Revised:2012-08-28 Online:2013-06-05 Published:2013-06-05
About author:*Corresponding author:Jiang Ling,Tel:027-87198493,E-mail:lingjiang@wipm.ac.cn.
Supported by:
国家自然科学基金资助项目（21173257，20921004）.

摘要/Abstract

摘要：

膜融合蛋白在介导膜融合过程中会发生构象的转变. 以同核2D NMR为手段，测定了pH 7.0条件下棉铃虫核多角体病毒(Helicoverpa armigera single- nucleocapsid Nucleopolyhedrovirus，HearNPV)的HaF融合肽在类膜环境中的3级结构. 通过与酸性条件下该融合肽的结构作比较，证实了该融合肽在从融合蛋白内部暴露出来到插入宿主细胞膜的过程中发生了构象的转变. 并且这个构象的转变是一个结构趋向稳定、两亲性趋向完整的变化过程. 这些结论对研究其他融合肽的插膜过程有普遍的意义，为探索膜融合机制提供了信息.

关键词: 核磁共振(NMR), 结构, 2D NMR, 杆状病毒融合肽

Abstract:

Fusion between viral and cellular membranes is an essential process for enveloped viruses to enter into cells. This process is usually mediated by fusion proteins on the surfaces of viral membranes. When pH changes from 7.0 to 5.0, the fusion proteins transform and expose their fusion peptide to anchor the cellular membrane and induce the subsequent fusion process. Ha133 (HaF) is the fusion protein of baculoviruse Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus (HearNPV). Its fusion peptide is composed of 20 residues, and located at the N-terminus of the F₁subunit. In this study, NMR methods were used to determine the solution structure of the fusion peptide in a membrane-mimicking environment at pH 7.0. It was found that the structure of the fusion peptide is composed of a 3₁₀ -helix from V⁷ to S⁹, a turn at V¹⁰, a regular α-helix from D¹¹ to G¹⁶ and two flexible coils at the N- and C-terminus. Comparing this structure to the available structure of this fusion peptide at pH 5.0, it is noted that, with decreasing pH, the conformation of the fusion peptide alters to be more stable and to have a more complete amphiphilic surface. These results should allow us to further investigate the mechanism of membrane fusion.

Key words: NMR, structure, fusion peptide, baculoviruse

中图分类号:

O482.53

曾丹云1,2，杜天鹏1,2，姜凌1*，刘买利1. 杆状病毒HaF融合肽在中性pH溶液中的NMR结构研究[J]. 波谱学杂志.

ZENG Dan-yun1,2, DU Tian-peng1,2, JIANG Ling1*, LIU Mai-li1. NMR Structure of Fusion Peptide of the Helicoverpa Armigera Single Nucleocapsid Nucleopolyhedrovirus F Protein at pH 7.0[J]. Chinese Journal of Magnetic Resonance.

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