Glutamylation of an HIV-1 protein inhibits the immune response by hijacking STING

	Glutamylation of an HIV-1 protein inhibits the immune response by hijacking STING
	Qian, G; Zhang, YH; Liu, YA; Li, MM; Xin, BW; Jiang, WY; Han, WD; Wang, Y; Tang, X; Li, LY; Zhu, LY; Sun, T; Yan, B; Zheng, YT; Xu, JQ; Ge, BX; Zhang, Z; Yan, DP
	2023
发表期刊	CELL REPORTS
ISSN	2211-1247
卷号	42 期号:5
摘要	Cyclic GMP-AMP synthase (cGAS) recognizes Y-form cDNA of human immunodeficiency virus type 1 (HIV-1) and initiates antiviral immune response through cGAS-stimulator of interferon genes (STING)-TBK1-IRF3-type I interferon (IFN-I) signalingcascade. Here, we report that the HIV-1 p6 protein suppresses HIV-1-stimulated expression of IFN-I and promotes immune evasion. Mechanistically, the glutamylated p6 at residue Glu6 in-hibits the interaction between STING and tripartite motif protein 32 (TRIM32) or autocrine motility factor recep-tor (AMFR). This subsequently suppresses the K27-and K63-linked polyubiquitination of STING at K337, there-fore inhibiting STING activation, whereas mutation of the Glu6 residue partially reverses the inhibitory effect. However, CoCl2, an agonist of cytosolic carboxypeptidases (CCPs), counteracts the glutamylation of p6 at the Glu6 residue and inhibits HIV-1 immune evasion. These findings reveal a mechanism through which an HIV-1 protein mediates immune evasion and provides a therapeutic drug candidate to treat HIV-1 infection.
收录类别	SCI
语种	英语
文献类型	期刊论文
条目标识符	http://ir.kiz.ac.cn/handle/152453/13968
专题	科研部门_分子免疫药理学（郑永唐）
推荐引用方式 GB/T 7714	Qian, G,Zhang, YH,Liu, YA,et al. Glutamylation of an HIV-1 protein inhibits the immune response by hijacking STING[J]. CELL REPORTS,2023,42(5).
APA	Qian, G.,Zhang, YH.,Liu, YA.,Li, MM.,Xin, BW.,...&Yan, DP.(2023).Glutamylation of an HIV-1 protein inhibits the immune response by hijacking STING.CELL REPORTS,42(5).
MLA	Qian, G,et al."Glutamylation of an HIV-1 protein inhibits the immune response by hijacking STING".CELL REPORTS 42.5(2023).

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
2024053163.pdf（7210KB）	期刊论文	出版稿	开放获取	CC BY-NC-SA	请求全文