Cowpea mosaic virus: From the presentation of antigenic peptides to the display of active biomaterials

被引:57
作者
Chatterji, A
Burns, LL
Taylor, SS
Lomonossoff, GP
Johnson, JE
Lin, T [1 ]
Porta, C
机构
[1] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Ctr Integrat Mol Biosci, La Jolla, CA 92037 USA
[3] Univ Calif San Diego, Dept Chem & Biochem, La Jolla, CA 92093 USA
[4] Hort Res Int Wellesbourne, Warwick, England
[5] John Innes Ctr, Dept Metab Biol, Norwich, Norfolk, England
关键词
plant virus-based chimeras; cowpea mosaic virus; human rhinovirus 14; chemical coupling of peptides to virus capsids; a kinase anchoring protein; general-purpose surface presentation system;
D O I
10.1159/000067929
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:362 / 370
页数:9
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