Heat shock proteins as ligands of toll-like receptors.
Heat shock proteins as ligands of toll-like receptors.
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DOI：
10.1007/978-3-642-59430-4_11
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发表时间：
2002
影响因子：
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通讯作者：
R. Vabulas;Hermann Wagner;H. Schild
中科院分区：
文献类型：
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作者：
R. Vabulas;Hermann Wagner;H. Schild
Toll 样受体 (TLR) 被描述为病原体相关分子模式的传感器，对于先天免疫反应的启动至关重要。这些机制早在适应性免疫系统进化之前就已形成。热休克蛋白 (HSP) 是不断增长的 TLR 配体列表中的最新成员。有趣的是，不仅细菌，哺乳动物 HSP 也与 TLR 相互作用，这表明 TLR 与微生物配体的排他性关联已经过时。人类 HSP60 和 Gp96 是非病原体衍生的 TLR 配体的第一个例子。更重要的是，Gp96 提供了第一个例子，说明如何通过在生理条件下从坏死细胞释放的相同分子同时刺激先天性和适应性免疫系统。了解先天免疫系统与热休克蛋白相互作用的机制将使合理调节免疫反应成为可能，无论是针对免疫还是针对耐受。
Toll-like receptors (TLRs) have been described as sensors for pathogen-associated molecular patterns crucial for the initiation of an innate immune response. These mechanisms were developed long before the adaptive immune system evolved. The latest additions to the growing list of TLR ligands are heat shock proteins (HSPs). Interestingly, not only bacterial but also mammalian HSPs interact with TLRs demonstrating that the exclusive association of TLRs with microbial ligands is obsolete. Human HSP60 and Gp96 are the first examples of non-pathogen derived ligands of TLRs. More importantly, Gp96 provides the first example of how the innate and adaptive immune system can be stimulated simultaneously by the same molecule which is released under physiological conditions from necrotic cells. Understanding the mechanisms of innate immune system interaction with HSPs will make it possible to rationally modulate immune responses, either towards immunity or towards tolerance.