Koga T, Wand-Württenberger A, DeBruyn J, Munk M E, Schoel B, Kaufmann S H
Department of Medical Microbiology and Immunology, University of Ulm, Federal Republic of Germany.
Science. 1989 Sep 8;245(4922):1112-5. doi: 10.1126/science.2788923.
Heat shock proteins are evolutionarily highly conserved polypeptides that are produced under a variety of stress conditions to preserve cellular functions. A major antigen of tubercle bacilli of 65 kilodaltons is a heat shock protein that has significant sequence similarity and cross-reactivity with antigens of various other microbes. Monoclonal antibodies against this common bacterial heat shock protein were used to identify a molecule of similar size in murine macrophages. Macrophages subjected to various stress stimuli including interferon-gamma activation and viral infection were recognized by class I-restricted CD8 T cells raised against the bacterial heat shock protein. These data suggest that heat shock proteins are processed in stressed host cells and that epitopes shared by heat shock proteins of bacterial and host origin are presented in the context of class I molecules.
热休克蛋白是进化上高度保守的多肽，在多种应激条件下产生以维持细胞功能。结核杆菌的一种主要的65千道尔顿抗原是一种热休克蛋白，它与各种其他微生物的抗原具有显著的序列相似性和交叉反应性。针对这种常见细菌热休克蛋白的单克隆抗体被用于鉴定小鼠巨噬细胞中一个大小相似的分子。受到包括γ干扰素激活和病毒感染在内的各种应激刺激的巨噬细胞，被针对细菌热休克蛋白产生的I类限制性CD8 T细胞识别。这些数据表明热休克蛋白在应激的宿主细胞中被加工处理，并且细菌和宿主来源的热休克蛋白共有的表位在I类分子的背景下呈递。
