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一类丝状噬菌体病毒的魔角旋转 NMR 研究。

Magic-angle spinning NMR of a class I filamentous bacteriophage virus.

机构信息

School of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Ramat Aviv 69978, Tel Aviv, Israel.

出版信息

J Phys Chem B. 2011 Aug 11;115(31):9671-80. doi: 10.1021/jp2040955. Epub 2011 Jul 19.

DOI:10.1021/jp2040955
PMID:21702439
Abstract

The fd bacteriophage is a filamentous virus that is widely used for bio- and nanotechnology applications ranging from phage display to battery materials. The possibility of obtaining a detailed description of its structural properties regardless of its state is therefore essential not only for understanding its physical arrangement and its bacterial infection process but also for many other applications. Here we present a study of the fd phage by magic-angle spinning solid-state NMR. While current structures rely on a Y21M mutant, experiments performed on a strain bearing a wild-type capsid report on high symmetry of the phage and lack of explicit subunit polymorphism. Chemical shift analysis confirmed that the coat protein mostly consists of a rigid right-handed curved α-helix (residues 6-47 of 50), preceded by a flexible loop-structured N-terminus. We were able to qualitatively assign the resonances belonging to the DNA, including the deoxyribose sugars and the thymine bases. These chemical shifts are consistent with base stacking and a C2'-endo/C3'-exo sugar pucker.

摘要

fd 噬菌体是一种丝状病毒,广泛应用于从噬菌体展示到电池材料的生物和纳米技术应用。因此,无论其状态如何,都有可能获得对其结构特性的详细描述,这不仅对于理解其物理排列和细菌感染过程至关重要,而且对于许多其他应用也至关重要。在这里,我们通过魔角旋转固态 NMR 研究了 fd 噬菌体。虽然目前的结构依赖于 Y21M 突变体,但在带有野生型衣壳的菌株上进行的实验报告了噬菌体的高对称性和缺乏明确的亚单位多态性。化学位移分析证实,外壳蛋白主要由刚性右手弯曲的α-螺旋(50 个残基中的 6-47)组成,前面是一个灵活的环结构 N 端。我们能够定性地分配属于 DNA 的共振,包括脱氧核糖糖和胸腺嘧啶碱基。这些化学位移与碱基堆积和 C2'-endo/C3'-exo 糖构象一致。

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