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细菌热休克蛋白与宿主细胞自身蛋白之间的表位同源性。

Epitope homology between bacterial heat shock protein and self-proteins in the host cell.

作者信息

Yamaguchi H, Yamamoto T, Konoeda Y, Taguchi H, Ogata S

机构信息

Department of Microbiology, Kyorin University School of Medicine, Tokyo, Japan.

出版信息

APMIS. 1992 Nov;100(11):957-62. doi: 10.1111/j.1699-0463.1992.tb04025.x.

Abstract

Mouse monoclonal antibodies (MAbs) showing distinct reactivity against the 60-kilodalton (kDa) antigen heat shock protein of Yersinia enterocolitica, designated cross-reacting protein antigen (CRPA), have previously been established. The reactivities of these MAbs (5C3 and 3C8) against mouse and human host cells were studied by Western blotting and flow cytometric analysis. The results indicated that epitopes on the bacterial 60-kDa heat shock protein are present on various molecules in mouse spleen cells and human B cells. An epitope recognized by MAb 5C3 was expressed on the mouse and human host cell surface, and an epitope recognized by MAb 3C8 was also expressed on the human host cell surface.

摘要

先前已制备出对小肠结肠炎耶尔森菌60千道尔顿(kDa)抗原热休克蛋白具有明显反应性的小鼠单克隆抗体(MAb),该抗原被称为交叉反应蛋白抗原(CRPA)。通过蛋白质印迹法和流式细胞术分析研究了这些单克隆抗体(5C3和3C8)对小鼠和人类宿主细胞的反应性。结果表明,细菌60-kDa热休克蛋白上的表位存在于小鼠脾细胞和人类B细胞的各种分子上。单克隆抗体5C3识别的一个表位在小鼠和人类宿主细胞表面表达,单克隆抗体3C8识别的一个表位也在人类宿主细胞表面表达。

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