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人T细胞识别的分枝杆菌热休克蛋白65表位包含不同结构。

Epitopes of the mycobacterial heat shock protein 65 for human T cells comprise different structures.

作者信息

Munk M E, Shinnick T M, Kaufmann S H

机构信息

Department of Medical Microbiology and Immunology, University of Ulm, Federal Republic of Germany.

出版信息

Immunobiology. 1990 Feb;180(2-3):272-7. doi: 10.1016/S0171-2985(11)80334-7.

Abstract

T cell recognition of foreign antigens is a result of a ternary complex between T cell receptor, nominal peptide and major histocompatibility complex molecule. It has been proposed that the nominal peptide, which is presented by accessory cells to T cells, has a characteristic structure which can be predicted on the basis of physicochemical criteria. To further study this aspect, we stimulated T cells from normal human blood donors with synthetic peptides (each of approximately 15 amino acids in length) from the heat shock protein 65 of Mycobacterium tuberculosis-M. bovis. We found that while the characterization of certain epitopes follows commonly used predictions, other epitopes cannot be predicted by known methods.

摘要

T细胞对外源抗原的识别是T细胞受体、名义肽和主要组织相容性复合体分子之间形成三元复合物的结果。有人提出,由辅助细胞呈递给T细胞的名义肽具有一种特征性结构,这种结构可以根据物理化学标准进行预测。为了进一步研究这方面,我们用来自结核分枝杆菌-牛分枝杆菌热休克蛋白65的合成肽(每个肽长度约为15个氨基酸)刺激正常人类献血者的T细胞。我们发现,虽然某些表位的特征符合常用的预测,但其他表位无法用已知方法预测。

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