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丝状噬菌体Pf1外壳蛋白的膜介导组装

Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein.

作者信息

Nambudripad R, Stark W, Opella S J, Makowski L

机构信息

Department of Physics, Boston University, MA 02215.

出版信息

Science. 1991 May 31;252(5010):1305-8. doi: 10.1126/science.1925543.

DOI:10.1126/science.1925543
PMID:1925543
Abstract

Filamentous bacteriophage Pf1 assembles by a membrane-mediated process during which the viral DNA is secreted through the membrane while being encapsulated by the major coat protein. Neutron diffraction studies showed that in the virus most of the coat protein consists of two alpha-helical segments arranged end-to-end with an intervening mobile surface loop. Nuclear magnetic resonance studies of the coat protein in the membrane-bound form have shown that the secondary structure is essentially identical to that in the intact virus. A comparison indicates that during membrane-mediated viral assembly, while the secondary structure of the coat protein is largely conserved, its tertiary structure changes substantially.

摘要

丝状噬菌体Pf1通过膜介导的过程进行组装,在此过程中,病毒DNA在通过膜分泌的同时被主要衣壳蛋白包裹。中子衍射研究表明,在病毒中,大部分衣壳蛋白由两个α-螺旋段组成,它们首尾相连,中间有一个可移动的表面环。对膜结合形式的衣壳蛋白进行的核磁共振研究表明,其二级结构与完整病毒中的基本相同。一项比较表明,在膜介导的病毒组装过程中,虽然衣壳蛋白的二级结构在很大程度上是保守的,但其三级结构发生了显著变化。

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