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来自结核分枝杆菌19-kDa抗原的小鼠T细胞刺激肽。与麻风分枝杆菌28-kDa蛋白的表位限制性同源性。

Murine T cell-stimulatory peptides from the 19-kDa antigen of Mycobacterium tuberculosis. Epitope-restricted homology with the 28-kDa protein of Mycobacterium leprae.

作者信息

Harris D P, Vordermeier H M, Roman E, Lathigra R, Brett S J, Moreno C, Ivanyi J

机构信息

MRC Tuberculosis and Related Infections Unit, Royal Postgraduate Medical School, London, UK.

出版信息

J Immunol. 1991 Oct 15;147(8):2706-12.

PMID:1717575
Abstract

Fifteen overlapping synthetic peptides, spanning the entire amino acid sequence of the Mycobacterium tuberculosis 19-kDa protein, were used to identify epitopes recognized by murine T cells. Five of the 15 peptides tested were able to elicit in vitro lymph node T cell proliferative responses in C57BL/10 mice primed by footpad inoculation with homologous peptide. Analysis in congenic strains of mice revealed H-2 restriction in the response to four peptides. However, one peptide, 19.7 (residues 61 to 80), induced T cell responses in all four haplotypes tested. This peptide was also unique in being able to stimulate lymph node cells from C57BL/10 mice immunized with recombinant 19-kDa protein, killed M. tuberculosis, or live bacillus Calmette Guerin infection. T cell lines specific for peptide 19.7 were of the CD4 phenotype. Significantly, sequence analysis revealed that residues 61 to 80 of the 19-kDa protein exhibited considerable homology with a single 20-amino acid sequence (residues 120 to 140), but not with any other region of the 28-kDa protein expressed in Mycobacterium leprae. This finding is the first evidence of epitope-restricted homology between otherwise structurally unrelated microbial Ag.

摘要

使用覆盖结核分枝杆菌19-kDa蛋白整个氨基酸序列的15个重叠合成肽来鉴定鼠T细胞识别的表位。在通过足垫接种同源肽进行免疫的C57BL/10小鼠中,所测试的15个肽中有5个能够引发体外淋巴结T细胞增殖反应。对同基因小鼠品系的分析揭示了对4个肽的反应存在H-2限制。然而,一个肽段19.7(第61至80位氨基酸残基)在所有测试的4种单倍型中均诱导T细胞反应。该肽段还具有独特之处,即能够刺激用重组19-kDa蛋白、经热灭活的结核分枝杆菌或活卡介苗感染免疫的C57BL/10小鼠的淋巴结细胞。针对肽段19.7的T细胞系表现为CD4表型。值得注意的是,序列分析显示,19-kDa蛋白的第61至80位氨基酸残基与一个单一的20个氨基酸序列(第120至140位氨基酸残基)具有相当的同源性,但与麻风分枝杆菌中表达的28-kDa蛋白的任何其他区域均无同源性。这一发现是结构上不相关的微生物抗原之间表位限制同源性的首个证据。

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