Wand-Württenberger A, Schoel B, Ivanyi J, Kaufmann S H
Department of Immunology, University of Ulm, FRG.
Eur J Immunol. 1991 Apr;21(4):1089-92. doi: 10.1002/eji.1830210437.
Bone marrow-derived macrophages were stained with a variety of monoclonal antibodies (mAb) with specificity for the mycobacterial heat shock protein (hsp) 60 or with specific rabbit antiserum raised against mycobacterial hsp 60. The mAb ML30 as well as the specific antiserum brightly stained bone marrow-derived macrophages whereas all the other mAb as well as normal rabbit antiserum gave no or negligible reactivity. Surface expression of the shared epitope is observed by day 3 of in vitro cultivation and markedly increased by interferon-gamma stimulation on day 9. Although hsp 60 is thought to be restricted to the mitochondrial compartment, antibody responses to this molecule have been implicated in autoimmunity. Our finding that bone marrow-derived macrophages express a cross-reactive epitope recognized by an mAb with specificity for amino acids 275 to 295 of the mycobacterial hsp 60 is consistent with such a role.
用多种对分枝杆菌热休克蛋白（hsp）60具有特异性的单克隆抗体（mAb）或用针对分枝杆菌hsp 60制备的特异性兔抗血清对骨髓来源的巨噬细胞进行染色。单克隆抗体ML30以及特异性抗血清能使骨髓来源的巨噬细胞呈现明亮染色，而所有其他单克隆抗体以及正常兔抗血清则无反应或反应可忽略不计。在体外培养的第3天可观察到共同表位的表面表达，在第9天经γ干扰素刺激后明显增加。尽管hsp 60被认为局限于线粒体区室，但对该分子的抗体反应已被认为与自身免疫有关。我们发现骨髓来源的巨噬细胞表达一种交叉反应性表位，该表位可被对分枝杆菌hsp 60第275至295位氨基酸具有特异性的单克隆抗体识别，这一发现与此种作用是一致的。
