Wang Shengnan, Li Jingwen, Miao Tiantian, Li Tuofan, Wan Zhimin, Xie Quan, Shao Hongxia, Qin Aijian, Ye Jianqiang
Key Laboratory of Jiangsu Preventive Veterinary Medicine, Key Laboratory for Avian Preventive Medicine, College of Veterinary Medicine, Ministry of Education, Yangzhou University, Yangzhou, Jiangsu, China 225009; Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, Jiangsu, China 225009; Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou, Jiangsu, China 225009.
Key Laboratory of Jiangsu Preventive Veterinary Medicine, Key Laboratory for Avian Preventive Medicine, College of Veterinary Medicine, Ministry of Education, Yangzhou University, Yangzhou, Jiangsu, China 225009; Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou, Jiangsu, China 225009; Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou, Jiangsu, China 225009; Institutes of Agricultural Science and Technology Development, Yangzhou University, Yangzhou, Jiangsu, China 225009.
Poult Sci. 2024 Dec;103(12):104272. doi: 10.1016/j.psj.2024.104272. Epub 2024 Aug 28.
In mammals, promyelocytic leukemia (PML) protein, also named as TRIM19, is the key component of nuclear membrane-less sub structures PML nuclear bodies (PML-NB) or nuclear domains 10 (ND10). PML-NBs are dynamic foci that consist of numerous permanently or transiently associated proteins. The mammalian PMLs are involved in the regulation of various cellular pathways, including apoptosis, intrinsic and innate antiviral immunity, cell cycle, DNA damage, senescence and etc. Nevertheless, little is known about the role of chicken PML (chPML). In this study, chPML gene was cloned, and its several functions were characterized. We found that chPML was widely expressed in different tissues of chickens, and showed different subcellular distribution pattern in DF-1 cells comparing with LMH and HD11 cells. Like human PML, chPML was identified to be SUMOylated. K463 is 1 critical SUMOylation site and RARRG is SUMO interaction motif (SIM) of chPML. Moreover, qPCR showed that chPML could not only up-regulate the expression of host innate immune factor IFN-β and its downstream ISGs, but also antigen presentation-related factors including class II transactivator (CIITA) and MHC II DM beta 2 (DMB2). Notably, over-expression of chIFN-β could promote the expression of endogenous chPML. All these provide novel insights into the function of chPML, and pave the way for further studying the roles of chPML in biological process and anti-infection function.
在哺乳动物中,早幼粒细胞白血病(PML)蛋白,也称为TRIM19,是无核膜亚结构PML核体(PML-NB)或核结构域10(ND10)的关键组成部分。PML-NB是动态病灶,由众多永久或暂时相关的蛋白质组成。哺乳动物的PML参与多种细胞途径的调节,包括细胞凋亡、固有和先天性抗病毒免疫、细胞周期、DNA损伤、衰老等。然而,关于鸡PML(chPML)的作用知之甚少。在本研究中,克隆了chPML基因,并对其多种功能进行了表征。我们发现chPML在鸡的不同组织中广泛表达,并且与LMH和HD11细胞相比,在DF-1细胞中显示出不同的亚细胞分布模式。与人类PML一样,chPML被鉴定为发生了SUMO化修饰。K463是chPML的一个关键SUMO化位点,RARRG是chPML的SUMO相互作用基序(SIM)。此外,qPCR表明chPML不仅可以上调宿主固有免疫因子IFN-β及其下游ISG的表达,还可以上调包括II类反式激活因子(CIITA)和MHC II DMβ2(DMB2)在内的抗原呈递相关因子的表达。值得注意的是,chIFN-β的过表达可以促进内源性chPML的表达。所有这些都为chPML的功能提供了新的见解,并为进一步研究chPML在生物学过程和抗感染功能中的作用铺平了道路。