Cowpea mosaic virus: From the presentation of antigenic peptides to the display of active biomaterials
Cowpea mosaic virus: From the presentation of antigenic peptides to the display of active biomaterials
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DOI：
10.1159/000067929
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发表时间：
2002-07-01
期刊：
影响因子：
4.6
通讯作者：
Porta, C
中科院分区：
文献类型：
--
作者：
Chatterji, A;Burns, LL;Porta, C
豇豆花叶病毒（CPMV），一种植物二十面体病毒，用于介绍外源肽和蛋白质的潜力。病毒表面最显著的特征是两种外壳蛋白中较小的一种（S）区域，该区域已被广泛用于插入外源肽。考虑到天然病毒的三维结构的可用性和表达外源肽的CPMV嵌合体对结晶的顺从性，免疫学数据可以与外源插入物的构象状态相关联。后者受到外来插入物内发生的蛋白水解的影响。在努力提供一个替代的背景下肽的表达，广泛的探索的第二个区域的S蛋白的报告相对于耐受小插入。此外，为了使CPMV适用于更宽的呈递谱，开发了一种技术以允许肽的表面偶联，所述肽可以用作一系列蛋白质的锚定点。这种新方法也广泛适用于肽和全长蛋白质结构域与病毒衣壳的直接化学交联。版权所有（C）2003 S. Karger AG，巴塞尔。
The potential of cowpea mosaic virus (CPMV), a plant icosahedral virus, for the presentation of foreign peptides and proteins is reported. The most prominent feature at the virus surface is a region of the smaller of the two coat proteins (S) which has been extensively used for the insertion of foreign peptides. Given the availability of the three-dimensional structure of the native virus and the amenability of foreign peptide-expressing CPMV chimeras to crystallisation, immunological data can be correlated with the conformational state of the foreign insert. The latter is influenced by proteolysis which occurs within the foreign inserts. In an effort to offer an alternative context for peptide expression, extensive exploration of a second region of the S protein is reported with respect to tolerance to small insertions. Moreover, to make CPMV suitable for a wider spectrum of presentation, a technique was developed to allow surface coupling of a peptide which can serve as the anchoring point for a range of proteins. This new approach is also widely applicable for the direct chemical cross-linking of peptides and full-length protein domains to the viral capsid. Copyright (C) 2003 S. Karger AG, Basel.