非洲猪瘟病毒及其编码蛋白 pEP153R 对自噬-溶酶体轴的调控

IF 2.8 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY Current Issues in Molecular Biology Pub Date : 2024-10-07 DOI:10.3390/cimb46100667
Si-Yu Bai, Wenlian Weng, Hua Wang, Zhiying Cui, Jiajun Wu, Yajin Qu, Yuxin Hao, Peng Gao, Yongning Zhang, Lei Zhou, Xinna Ge, Xin Guo, Jun Han, Hanchun Yang
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引用次数: 0

摘要

自噬-溶酶体轴是一种进化保守的细胞内降解途径,是宿主先天免疫抵抗微生物感染的重要组成部分。在这里,我们发现非洲猪瘟病毒(ASFV)是对全球养猪业最具破坏性的病原体之一,它可以通过将关键的溶酶体膜蛋白(LAMP1 和 LAMP2)招募到病毒工厂来重塑自噬-溶酶体轴,同时抑制巨噬细胞中的自噬诱导。对病毒膜蛋白的筛选发现了几种 ASFV 膜蛋白,如病毒蛋白 pEP153R,当其在转染细胞中单独表达时,可显著改变 LAMP1/2 的亚细胞定位。进一步的分析表明,pEP153R 也是病毒工厂的一个组成部分,可以诱导内质网(ER)保留 LAMP1/2,从而抑制自噬体与溶酶体的融合。有趣的是,缺乏EP153R的ASFV突变体仍能积极招募LAMP进入病毒工厂(VFs)并抑制自噬通量,这表明在pEP153R缺失的情况下存在其他病毒蛋白的功能冗余,凸显了ASFV复制生物学的复杂性。综上所述,我们的研究结果揭示了 ASFV 与自噬-溶酶体轴相互作用的新信息,以及 ASFV 蛋白 pEP153R 在调节细胞自噬过程中的一种先前未被认识到的功能。
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Modulation of Autophagy-Lysosome Axis by African Swine Fever Virus and Its Encoded Protein pEP153R.

The autophagy-lysosome axis is an evolutionarily conserved intracellular degradation pathway which constitutes an important component of host innate immunity against microbial infections. Here, we show that African swine fever virus (ASFV), one of most devastating pathogens to the worldwide swine industry, can reshape the autophagy-lysosome axis by recruiting the critical lysosome membrane proteins (LAMP1 and LAMP2) to viral factories while inhibiting autophagic induction in macrophages. The screening of viral membrane proteins led to the identification of several ASFV membrane proteins, exemplified by viral protein pEP153R, that could significantly alter the subcellular localization of LAMP1/2 when expressed alone in transfected cells. Further analysis showed that pEP153R was also a component of viral factories and could induce endoplasmic reticulum (ER) retention of LAMP1/2, leading to the inhibition of the fusion of autophagosomes with lysosomes. Interestingly, the ASFV mutant lacking EP153R could still actively recruit LAMP into viral factories (VFs) and inhibit autophagic flux, indicating the existence of a functional redundancy of other viral proteins in the absence of pEP153R and highlighting the complexity of ASFV replication biology. Taken together, our results reveal novel information about the interplay of ASFV with the autophagy-lysosome axis and a previously unrecognized function of ASFV protein pEP153R in regulating the cellular autophagic process.

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来源期刊
Current Issues in Molecular Biology
Current Issues in Molecular Biology 生物-生化研究方法
CiteScore
2.90
自引率
3.20%
发文量
380
审稿时长
>12 weeks
期刊介绍: Current Issues in Molecular Biology (CIMB) is a peer-reviewed journal publishing review articles and minireviews in all areas of molecular biology and microbiology. Submitted articles are subject to an Article Processing Charge (APC) and are open access immediately upon publication. All manuscripts undergo a peer-review process.
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