Next Article in Journal
Fluorescence Microscopy of the HIV-1 Envelope
Previous Article in Journal
Non-Coding RNAs and Their Role in Respiratory Syncytial Virus (RSV) and Human Metapneumovirus (hMPV) Infections
Open AccessArticle

The E3 Ubiquitin Ligase TRIM21 Promotes HBV DNA Polymerase Degradation

Tianjin Life Science Research Center, Tianjin Key Laboratory of Inflammation Biology, Collaborative Innovation Center of Tianjin for Medical Epigenetics, Department of Pathogen Biology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin 30070, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2020, 12(3), 346; https://doi.org/10.3390/v12030346
Received: 10 February 2020 / Revised: 18 March 2020 / Accepted: 19 March 2020 / Published: 21 March 2020
(This article belongs to the Section Animal Viruses)
The tripartite motif (TRIM) protein family is an E3 ubiquitin ligase family. Recent reports have indicated that some TRIM proteins have antiviral functions, especially against retroviruses. However, most studies mainly focus on the relationship between TRIM21 and interferon or other antiviral effectors. The effect of TRIM21 on virus-encoded proteins remains unclear. In this study, we screened candidate interacting proteins of HBV DNA polymerase (Pol) by FLAG affinity purification and mass spectrometry assay and identified TRIM21 as its regulator. We used a coimmunoprecipitation (co-IP) assay to demonstrate that TRIM21 interacted with the TP domain of HBV DNA Pol. In addition, TRIM21 promoted the ubiquitination and degradation of HBV DNA Pol using its RING domain, which has E3 ubiquitin ligase activity. Lys260 and Lys283 of HBV DNA Pol were identified as targets for ubiquitination mediated by TRIM21. Finally, we uncovered that TRIM21 degrades HBV DNA Pol to restrict HBV DNA replication, and its SPRY domain is critical for this activity. Taken together, our results indicate that TRIM21 suppresses HBV DNA replication mainly by promoting the ubiquitination of HBV DNA Pol, which may provide a new potential target for the treatment of HBV. View Full-Text
Keywords: hepatitis B virus; TRIM21; HBV DNA Pol; interaction; ubiquitination hepatitis B virus; TRIM21; HBV DNA Pol; interaction; ubiquitination
Show Figures

Figure 1

MDPI and ACS Style

Mu, T.; Zhao, X.; Zhu, Y.; Fan, H.; Tang, H. The E3 Ubiquitin Ligase TRIM21 Promotes HBV DNA Polymerase Degradation. Viruses 2020, 12, 346. https://doi.org/10.3390/v12030346

AMA Style

Mu T, Zhao X, Zhu Y, Fan H, Tang H. The E3 Ubiquitin Ligase TRIM21 Promotes HBV DNA Polymerase Degradation. Viruses. 2020; 12(3):346. https://doi.org/10.3390/v12030346

Chicago/Turabian Style

Mu, Ting; Zhao, Xiaoqing; Zhu, Yanan; Fan, Hongxia; Tang, Hua. 2020. "The E3 Ubiquitin Ligase TRIM21 Promotes HBV DNA Polymerase Degradation" Viruses 12, no. 3: 346. https://doi.org/10.3390/v12030346

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop