大肠杆菌噬菌体MS2 A蛋白的定位

Localization of coliphage MS2 A-protein.

作者信息

Curtiss L K, Krueger R G

出版信息

J Virol. 1974 Sep;14(3):503-8. doi: 10.1128/JVI.14.3.503-508.1974.

DOI:10.1128/JVI.14.3.503-508.1974

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC355543/

Abstract

The purification of coliphage MS2 dinitrophenol (DNP) conjugates provided a system for localization of the single molecule of A-protein in the capsid of the MS2 phage particle. Three A-protein preparations isolated from unconjugated MS2, overconjugated DNP-MS2, and purified 78S DNP-MS2 were tested for the presence of covalently bound DNP. The binding characteristics to Dowex 1-X8 and rabbit anti-DNP bovine serum albumin (DNP-BSA) immunoglobulin G of the 78S DNP-MS2 and overconjugated DNP-MS2 A-protein preparations indicate that the A-protein is located on the surface of the phage particle where it can be covalently conjugated with hapten. Extensive enzymatic iodination of the A-protein of intact unconjugated MS2 substantiates this conclusion.

摘要

大肠杆菌噬菌体MS2二硝基苯酚（DNP）缀合物的纯化提供了一个用于在MS2噬菌体颗粒衣壳中定位单个A蛋白分子的系统。对从未缀合的MS2、过度缀合的DNP-MS2和纯化的78S DNP-MS2中分离出的三种A蛋白制剂进行了共价结合DNP的检测。78S DNP-MS2和过度缀合的DNP-MS2 A蛋白制剂与Dowex 1-X8以及兔抗DNP牛血清白蛋白（DNP-BSA）免疫球蛋白G的结合特性表明，A蛋白位于噬菌体颗粒表面，在那里它可以与半抗原共价缀合。完整未缀合MS2的A蛋白的广泛酶促碘化证实了这一结论。

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