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呼肠孤病毒3型的σ1蛋白是多聚体的证据。

Evidence that the sigma 1 protein of reovirus serotype 3 is a multimer.

作者信息

Bassel-Duby R, Nibert M L, Homcy C J, Fields B N, Sawutz D G

出版信息

J Virol. 1987 Jun;61(6):1834-41. doi: 10.1128/JVI.61.6.1834-1841.1987.

DOI:10.1128/JVI.61.6.1834-1841.1987
PMID:3553613
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC254187/
Abstract

In this report, we study the reovirus serotype 3 (strain Dearing) sigma 1 protein obtained from various sources: from Escherichia coli expressing sigma 1 protein, from reovirus-infected mouse L cells, and from purified reovirions. We demonstrate that the sigma 1 protein is a multimer in its undisrupted form and present biochemical evidence suggesting that the multimer is made up of four sigma 1 subunits.

摘要

在本报告中，我们研究了从多种来源获得的呼肠孤病毒3型（迪林毒株）σ1蛋白：从表达σ1蛋白的大肠杆菌中获得、从感染呼肠孤病毒的小鼠L细胞中获得以及从纯化的呼肠孤病毒颗粒中获得。我们证明，σ1蛋白在其未破坏的形式下是一种多聚体，并提供了生化证据表明该多聚体由四个σ1亚基组成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/db1bf73da51c/jvirol00097-0083-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/fc8a0b17020e/jvirol00097-0080-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/3daf0f2b62d2/jvirol00097-0080-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/dbf70ce8fcb2/jvirol00097-0081-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/367a46dcf544/jvirol00097-0081-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/37330fc80003/jvirol00097-0082-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/9a3e4e289b0d/jvirol00097-0082-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/db1bf73da51c/jvirol00097-0083-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/fc8a0b17020e/jvirol00097-0080-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/3daf0f2b62d2/jvirol00097-0080-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/dbf70ce8fcb2/jvirol00097-0081-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/367a46dcf544/jvirol00097-0081-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/37330fc80003/jvirol00097-0082-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/9a3e4e289b0d/jvirol00097-0082-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ea80/254187/db1bf73da51c/jvirol00097-0083-a.jpg

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引用本文的文献

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Identification of carbohydrate-binding domains in the attachment proteins of type 1 and type 3 reoviruses.1型和3型呼肠孤病毒附着蛋白中碳水化合物结合结构域的鉴定。
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2
Cleavage susceptibility of reovirus attachment protein sigma1 during proteolytic disassembly of virions is determined by a sequence polymorphism in the sigma1 neck.呼肠孤病毒附着蛋白σ1在病毒粒子蛋白水解性解体过程中的切割敏感性由σ1颈部的序列多态性决定。
J Virol. 1998 Oct;72(10):8205-13. doi: 10.1128/JVI.72.10.8205-8213.1998.
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Protein architecture of avian reovirus S1133 and identification of the cell attachment protein.

本文引用的文献

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Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles.哺乳动物呼肠孤病毒的西格玛1蛋白从病毒颗粒表面伸出。
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Inhibition of cellular DNA synthesis by reovirus occurs through a receptor-linked signaling pathway that is mimicked by antiidiotypic, antireceptor antibody.呼肠孤病毒对细胞DNA合成的抑制作用是通过一种受体连接信号通路实现的，抗独特型、抗受体抗体可模拟该信号通路。
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Periodic charge distributions in the myosin rod amino acid sequence match cross-bridge spacings in muscle.肌球蛋白杆状氨基酸序列中的周期性电荷分布与肌肉中的横桥间距相匹配。
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Biochemical studies on the mechanism of chemical and physical inactivation of reovirus.呼肠孤病毒化学和物理灭活机制的生化研究
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Streptococcal M protein: alpha-helical coiled-coil structure and arrangement on the cell surface.链球菌M蛋白：α-螺旋卷曲螺旋结构及其在细胞表面的排列
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