Structural and functional characterization of peptide-beta2m fused HLA-A2/MART1(27-35) complexes.
Structural and functional characterization of peptide-beta2m fused HLA-A2/MART1(27-35) complexes.
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发表时间:
2006
影响因子:
3.1
通讯作者:
Chuanlai Shen;Chien-Chung Chang;Jianqiong Zhang;W. Guo;Lingzhi Xia;F. Meng;W. Xie
中科院分区:
文献类型:
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作者:
Chuanlai Shen;Chien-Chung Chang;Jianqiong Zhang;W. Guo;Lingzhi Xia;F. Meng;W. Xie
The uses of soluble HLA class I/peptide complexes to monitor antigen reactive T cells are often hampered by their low-yield and high-cost production. As an alternative strategy, the peptide-beta(2)m fused, 2-component (2C) HLA class I/peptide complex has been developed, but its application is limited due to the lack of the comparison of its structural and functional characteristics with those of its conventional 3-component (3C) counterpart. In this study, we have demonstrated that the 2C and 3C HLA-A2/MART1(27-35) complexes have a similar chromatographical profile and comparable stability, but the former has 2.5 times higher yield and significantly higher binding ability with HLA-A2/MART1(27-35) complex-specific receptors than the latter. Furthermore, the 2C complex has a comparable ability to stimulate specific CTL proliferation, but appears to be more effective in eliciting the cytotoxicity of antigen-specific CTL, as compared to its 3C counterpart.