Covalent linkage to beta2-microglobulin enhances the MHC stability and antigenicity of suboptimal CTL epitopes.

Covalent linkage to beta2-microglobulin enhances the MHC stability and antigenicity of suboptimal CTL epitopes.
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与 β2-微球蛋白的共价连接增强了 MHC 稳定性和次优 CTL 表位的抗原性。

DOI:
10.4049/jimmunol.162.10.6024
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发表时间:
1999
影响因子:
4.4
通讯作者:
B. Barber
B. Barber
中科院分区:
医学2区
文献类型:
--
作者:
R. Uger;S. M. Chan;B. Barber

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Many CTL epitopes of clinical importance, particularly those derived from tumor Ags, display relatively poor MHC binding affinity and stability. Because in vivo immunogenicity, and thus the efficacy of peptide-based vaccines, is thought to be determined by MHC/peptide complex stability, there is a need to develop a simple strategy for enhancing the binding of suboptimal epitopes. Toward this goal, the ability to enhance suboptimal peptides through covalent linkage to beta2-microglobulin (beta2m) was explored. Two suboptimal variants of a high-affinity Db-restricted influenza nucleoprotein peptide were covalently linked, via a polypeptide spacer, to the amino terminus of human beta2m and the recombinant fusion proteins expressed in Escherichia coli. When compared with their uncoupled counterparts, the beta2m-linked epitopes display enhanced MHC stabilization and antigenicity. Thus, tethering epitopes to beta2m provides a simple method for augmenting the biological activity of suboptimal peptides and could be useful in the design of peptide-based vaccines or immunotherapeutics.
与 β2-微球蛋白的重新结合对于外源流感肽的 Db I 类主要组织相容性复合物结合是必要的。
DOI: 10.1073/pnas.88.1.301
发表时间: 1991
影响因子: 11.1
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DOI: --
发表时间: 1993
期刊: Journal of immunology (Baltimore, Md. : 1950)
影响因子: --
作者:
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DOI: 10.4049/jimmunol.154.11.5934
发表时间: 1995-06
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对表达 H-2Db 但不表达 H-2Kb 或 β2-微球蛋白的 EL4 细胞系进行分子分析。
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影响因子: 11.1
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