Hepatitis B virus (HBV) infection is one of the most important infectious diseases in China. In this study, we investigated the functional role of miR-137 in HBV infection to further elucidate the mechanism underlying the associated pathology. Viral replication was determined after transfection of HEK293 cells with the replication-competent vector pHBV1.3 and miR137 mimics or inhibitors. Expression of HBV genes was determined by quantitative real-time PCR (qRT-PCR). Expression of miR-137 and protein inhibitor of activated STAT 2 (PIAS2) was determined by qRT-PCR and Western blotting. Activity of the PIAS2 3'-UTR was determined by dual-luciferase reporter assays. Transfection of HEK293 cells with pHBV1.3 increased the expression of miR-137. Co-transfection with miR-137 mimic upregulated HBV gene expression and viral replication. MiR-137 targeted the PIAS2 3'-UTR, and suppressed PIAS2 mRNA and protein expressions. SiRNA-mediated PIAS2 knockdown suppressed HBV gene expression and viral replication. PIAS2 expression rescued the promotion effect of miR-137 on HBV expression and viral replication. MiR-137 expression was significantly upregulated following HBV infection. Furthermore, miR-137 promoted the expression of HBV genes and viral replication by targeting the expression of PIAS2. Our findings might provide a new insight into the diagnosis and treatment of HBV infection.

Download full-text PDF

Source
http://dx.doi.org/10.1691/ph.2017.7594DOI Listing

Publication Analysis

Top Keywords

viral replication
20
hbv infection
16
gene expression
12
expression viral
12
expression
11
hbv
9
hepatitis virus
8
replication targeting
8
protein inhibitor
8
inhibitor activated
8

Similar Publications

Proteomic analysis of the nonstructural protein 2-host protein interactome reveals a novel regulatory role of SH3 domain-containing kinase-binding protein 1 in porcine reproductive and respiratory syndrome virus replication and apoptosis.

Int J Biol Macromol

January 2025

College of Veterinary Medicine, South China Agricultural University, Guangzhou 510642, China; Zhaoqing Branch Centre of Guangdong Laboratory for Lingnan Modern Agricultural Science and Technology, Zhaoqing 526238, China; Zhaoqing Institute of Biotechnology Co., Ltd., Zhaoqing 526238, China; Guangdong Wens Dahuanong Bio-Pharmaceutical Co., Ltd., Xinxing 527400, China. Electronic address:

Virus-host protein interaction is critical for successful completion of viral replication cycles. As the largest nonstructural protein (NSP) of porcine reproductive and respiratory syndrome virus (PRRSV), NSP2 plays multiple and critical roles in viral replication, antiviral immunity, cellular tropism and virulence. An interactome of this protein with host proteins would be instrumental in full understanding of these multifunctional roles.

View Article and Find Full Text PDF

RAP1 is essential for PRRSV replication and the synthesis of the viral genome.

Vet Microbiol

December 2024

Guangdong Provincial Key Laboratory of Zoonosis Prevention and Control, College of Veterinary Medicine, South China Agricultural University, Guangzhou 510462, China; National Engineering Research Center for Breeding Swine Industry, South China Agricultural University, Guangzhou 510642, China. Electronic address:

Since its emergence, porcine reproductive and respiratory syndrome (PRRS) has caused enormous economic losses to the global swine industry. The pathogenesis of PRRS remains under investigation. The porcine reproductive and respiratory syndrome virus (PRRSV) causes reproductive disorders in pigs and respiratory in piglets, which is a 15 kb RNA virus that encodes 16 viral proteins, most of which exhibit multiple functions during the virus lifecycle.

View Article and Find Full Text PDF

Multiple sphingolipid-metabolizing enzymes modulate influenza virus replication.

Virology

December 2024

Departments of Surgery & Molecular Microbiology and Immunology, University of Missouri, Columbia, MO, 65212, USA. Electronic address:

The sphingolipid network is sustained principally by the balance of bioactive sphingolipid molecules and their regulation by sphingolipid-metabolizing enzymes. The components in the lipid system display key functions in numerous cellular and disease conditions including virus infections. During the COVID-19 pandemic, there was a fruitful effort to use an inhibitor that blocks the activity of sphingosine kinase (SphK) 2 to cure the devastating disease.

View Article and Find Full Text PDF

Imaging of viral replication in live cells by using split fluorescent protein-tagged reporter flaviviruses.

Virology

December 2024

The Centre for Infection and Immunity Studies, School of Medicine, Sun Yat-sen University, Shenzhen, Guangdong, 518107, China. Electronic address:

The knowledge on the life cycle of flaviviruses is still incomplete, and no direct-acting antivirals against their infections are clinically available. Herein, by screening via a Zika virus (ZIKV) replicon assay, we found that the N-terminus of NS2A exhibited great tolerance to the insertions of different split fluorescent proteins (split-FPs). Furthermore, both ZIKV and dengue virus encoding a split-FP-tagged NS2A propagated efficiently, and the split-FP-tagged ZIKVs had good genetic stability.

View Article and Find Full Text PDF

A Novel Protein NLRP12-119aa that Prevents Rhabdovirus Replication by Disrupting the RNP Complex Formation.

Adv Sci (Weinh)

January 2025

Laboratory of Fish Molecular Immunology, College of Fisheries and Life Science, Shanghai Ocean University, Shanghai, 201306, China.

The accurate assembly of the ribonucleoprotein (RNP) complex is fundamental for the replication and transcription of rhabdoviruses, which are known for their broad pathogenic impact. A novel 119-amino-acid protein, NLRP12-119aa is identified, encoded by the circular RNA circNLRP12, that effectively disrupts the formation of rhabdovirus RNP complexes through two distinct mechanisms and significantly reduces their replication. NLRP12-119aa exhibits a strong affinity for the conserved 18-nucleotide sequence at the start of the leader RNA of rhabdoviruses VSV, SCRV, and RABV, outcompeting their native N protein interactions, thereby disrupting the assembly of RNP complexes and inhibiting viral replication.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!