Human immunodeficiency virus in total hip arthroplasty.

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Abstract

Conflict of interest statement: ICMJE Conflict of interest statement: LM reports consultancy for Zimmerbiomet and Implantcast; payment for lectures including service on speakers’ bureaus for Zimmerbiomet, Smith and Nephew and Advanced Orthopaedics, all outside the submitted work. The other authors declare no conflict of interest relevant to this work. 11. Viruses. 2025 Feb 14;17(2):260. doi: 10.3390/v17020260. The Deubiquitinase OTUD1 Influences HIV-1 Release by Regulating the Host Restriction Factor BST-2. Zhang MD(1)(2)(3), Chen F(2)(3), He WQ(1)(4), Lu Y(1), Liu FL(1), Zhang HG(3), Yang LM(1), Dong CS(3), Xiong SD(2)(3), Zheng YT(1)(2). Author information: (1)State Key Laboratory of Genetic Evolution & Animal Models, Key Laboratory of Bioactive Peptides of Yunnan Province, KIZ-CUHK Joint Laboratory of Bioresources and Molecular Research in Common Diseases, Center for Biosafety Mega-Science, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, China. (2)KIZ-SU Joint Laboratory of Animal Model and Drug Development, College of Pharmaceutical Sciences, Soochow University, Suzhou 215021, China. (3)Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou 215021, China. (4)University of Chinese Academy of Sciences, Beijing 100049, China. Bone marrow stromal cell antigen 2 (BST-2) is a restriction factor for human immunodeficiency virus type I (HIV-1) and plays an important role in regulating the release of viral particles. However, the antiviral efficacy of BST-2 is antagonized by the HIV-1-encoded accessory protein Vpu, which facilitates the degradation of BST-2 by recruiting E3 ubiquitin ligase β-TrCP. The involvement of deubiquitinases (DUBs) in counteracting BST-2 ubiquitination and influencing its stability during HIV-1 infection remains inadequately explored. In this study, we conducted a small interfering RNA (siRNA) screening of human DUBs and determined that OTUD1 interacts with BST-2, leading to a reduction in its K48- and K63-linked ubiquitination. This reduction increases BST-2 protein stability, and subsequently inhibits HIV-1 release. Our findings reveal a novel regulatory mechanism by which DUBs influence the stability of the HIV-1 restriction factor BST-2 to dampen viral release, providing a potential therapeutic target for HIV-1 antiviral intervention. DOI: 10.3390/v17020260 PMCID: PMC11860778