RNF152 regulates prototype foamy virus replication by targeting Gag polyubiquitination and VLPs production

Lin Jiang; Xinhong Tian; Keran Ma; Wentao Qiao; Juan Tan

doi:10.1016/j.virs.2026.08.016

October 2026

. doi: 10.1016/j.virs.2026.08.016

Citation: Lin Jiang, Xinhong Tian, Keran Ma, Wentao Qiao, Juan Tan. RNF152 regulates prototype foamy virus replication by targeting Gag polyubiquitination and VLPs production .VIROLOGICA SINICA, 2026, 41(5) : 1078-1090. http://dx.doi.org/10.1016/j.virs.2026.08.016

环指蛋白152通过降解原型泡沫病毒Gag蛋白及减少病毒颗粒生成抑制病毒复制

南开大学, 生命科学学院, 分子微生物与技术教育部重点实验室

通讯作者： 乔文涛, wentaoqiao@nankai.edu.cn; 谈娟, juantan@nankai.edu.cn
收稿日期： 2026-03-18
录用日期： 2026-08-31

摘要

泡沫病毒（Foamy viruses，FVs）属于反转录病毒科、泡沫病毒亚科、泡沫病毒属。原型泡沫病毒（Prototype foamy virus，PFV）是FVs的代表性成员，可在宿主体内建立长期潜伏感染且不致病，这一特性使其可能成为极具潜力的基因转移载体。深入了解宿主与PFV复制的相互关系及机制，是全面了解FVs生物学特征以及提高FVs载体基因转移效率的理论基础。目前已知能够调控PFV复制的宿主蛋白数量较为有限。分析前期PFV感染HT1080细胞后的转录组学结果，观察到环指蛋白152（RING finger protein 152，RNF152）在调节PFV复制中的潜在作用。由此展开RNF152影响PFV复制的功能与机制研究，发现在HT1080细胞中过表达RNF152会显著抑制PFV复制，而敲减HT1080细胞内源RNF152则显著促进PFV复制。由于RNF152属于泛素连接酶，其主要功能为介导底物蛋白的泛素化修饰，基于此，本文发现PFV Gag可作为RNF152的底物蛋白，与RNF152相互作用。RNF152可介导PFV Gag K396处的泛素化修饰，导致其通过蛋白酶体途径降解。RNF152还通过非泛素化依赖途径影响PFV Gag的多聚化以及Env-Gag的相互作用，导致PFV毒粒粒径减小、释放减少。这些发现首次阐明了RNF152在病毒复制中的作用，深化病毒与宿主相互作用的认识，为解释反转录病毒的复制机制提供新视角，有助于提高基于反转录病毒改造载体的基因转移效率，同时也可能为发现新的防控反转录病毒感染的方法和手段提供借鉴。
- 原型泡沫病毒
- , 环指蛋白152
- , Gag
- , 病毒样颗粒

RNF152 regulates prototype foamy virus replication by targeting Gag polyubiquitination and VLPs production

Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin 300071, China

Corresponding author: Wentao Qiao, wentaoqiao@nankai.edu.cn Juan Tan, juantan@nankai.edu.cn
Received Date: 18 March 2026
Accepted Date: 31 August 2026

Abstract

Prototype foamy viruses (PFVs) are complex retroviruses that establish long-term latent infections in hosts without causing disease, positioning them as potential safe gene transfer vectors. Understanding the host proteins involved in PFV replication and their interaction mechanisms may enhance gene transfer efficiency. However, only a few cellular proteins are known to influence PFV replication. Based on the transcriptomic analysis of PFV-infected HT1080 cells, we observed a potential significance of RING finger protein 152 (RNF152) in modulating PFV replication. Overexpression of RNF152 significantly inhibits PFV replication, whereas RNF152 knockdown enhances viral replication. Mechanistically, RNF152 interacts with the Gag protein to promote its polyubiquitination at lysine 396 (K396), thereby facilitating its degradation via the ubiquitin-proteasome system. Furthermore, RNF152 reduces the size and number of PFV virus-like particles (VLPs) by inhibiting the multimerization of Gag. Collectively, our findings reveal a previously unrecognized mechanism that influences PFV infection. Additionally, we elucidate the role of RNF152 in affecting virus replication for the first time, providing valuable insights into the mechanisms of virus replication and demonstrating the importance of ubiquitination modification in affecting viral replication.
- Prototype foamy virus (PFV)
- , RING finger protein 152 (RNF152)
- , Gag
- , Virus-like particles (VLPs)

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