LMP7 通过与 NLRP3 相互作用抑制 NLRP3 炎性小体的激活。
LMP7 inhibits the activation of NLRP3 inflammasome through interaction with NLRP3.
机构信息
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Key Laboratory of Virology of Guangzhou, Institute of Medical Microbiology, Jinan University, Guangzhou, 510632, China.
出版信息
Biochem Biophys Res Commun. 2020 Oct 15;531(2):152-159. doi: 10.1016/j.bbrc.2020.07.091. Epub 2020 Aug 8.
The innate immune system recognizes pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs) by coding pattern recognition receptors (PRRs). As a well-known inflammasome, NLRP3 plays an essential role in helping the host immune response and driving antiviral processes. Low molecular mass polypeptide (LMP7) is a critical component of the immunoproteasome that participates in host antiviral activity, as well as T cell function and development. This is the first study to report the direct interaction between LMP7 and NLRP3. Also, LMP7 was found to inhibit the activation of the NLRP3 inflammasome, which is of great significance in exploring the role of the immune proteasome in regulating the activation of NLRP3.
天然免疫系统通过编码模式识别受体（PRRs）识别病原体相关分子模式（PAMPs）和损伤相关分子模式（DAMPs）。作为一种众所周知的炎症小体，NLRP3 在帮助宿主免疫反应和驱动抗病毒过程中发挥着重要作用。低分子量多肽（LMP7）是免疫蛋白酶体的关键组成部分，参与宿主抗病毒活性以及 T 细胞功能和发育。这是首次报道 LMP7 与 NLRP3 之间的直接相互作用的研究。此外，发现 LMP7 抑制 NLRP3 炎症小体的激活，这对于探索免疫蛋白酶体在调节 NLRP3 激活中的作用具有重要意义。
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