Category Ranking
98%
Total Visits
921
Avg Visit Duration
2 minutes
Citations
20
Article Abstract
The ubiquitination process is a reversible posttranslational modification involved in many essential cellular functions, such as innate immunity, cell signaling, trafficking, protein stability, and protein degradation. Viruses can use the ubiquitin system to efficiently enter host cells, replicate and evade host immunity, ultimately enhancing viral pathogenesis. Emerging evidence indicates that enveloped viruses can carry free (unanchored) ubiquitin or covalently ubiquitinated viral structural proteins that can increase the efficiency of viral entry into host cells. Furthermore, viruses continuously evolve and adapt to take advantage of the host ubiquitin machinery, highlighting its importance during virus infection. This review discusses the battle between viruses and hosts, focusing on how viruses hijack the ubiquitination process at different steps of the replication cycle, with a specific emphasis on viral entry. We discuss how ubiquitination of viral proteins may affect tropism and explore emerging therapeutics strategies targeting the ubiquitin system for antiviral drug discovery.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/bs.aivir.2024.05.001 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Identification of multifunctional T-cell peptide epitopes for the development of DNA vaccines against dengue virus.
Hum Vaccin Immunother
December 2025
Beijing Institute of Tropical Medicine, Beijing Friendship Hospital, Capital Medical University, Beijing Key Laboratory for Research on Prevention and Treatment of Tropical Diseases, Beijing, China.
Dengue virus (DENV) is an important arthropod-borne virus that poses a global health threat, with half of the world's population at risk of infection. Currently, there is a lack of safe and effective vaccines for its prevention. Antibody-dependent enhancement (ADE) occurs when cross-reactive antibodies fail to neutralize heterologous DENV serotypes effectively, facilitating viral entry into Fc receptor-bearing cells and leading to more severe disease.
View Article and Find Full Text PDFInteraction between W41 of the hepatitis B virus preS1 surface peptide and Y146/F274 of the cellular receptor molecule Na/taurocholate co-transporting polypeptide is essential for virus entry.
Mol Pharmacol
August 2025
Institute of Pharmacology and Toxicology, Faculty of Veterinary Medicine, Biomedical Research Center Seltersberg, Justus Liebig University of Giessen, Giessen, Germany. Electronic address:
The myristoylated preS1 domain (myr-preS1) of the hepatitis B virus (HBV) large surface protein is essential for binding to the receptor protein, Na/taurocholate co-transporting polypeptide (NTCP), and for the subsequent internalization of the virus-receptor complex. NTCP, which is expressed in hepatocytes, plays a physiological role in hepatic bile acid transport. Recent cryo-electron microscopy structures of the myr-preS1-NTCP complex were used to analyze virus-receptor interactions at the molecular level.
View Article and Find Full Text PDFCharacterisation of a secreted MFSD6-Fc microbody as a decoy receptor for respiratory enterovirus D68.
EBioMedicine
September 2025
Cancer Centre, The First Hospital of Jilin University, Changchun, Jilin, 130021, China; Institute of Virology and AIDS Research, The First Hospital of Jilin University, Changchun, Jilin, 130021, China; Institute of Translational Medicine, Key Laboratory of Organ Regeneration and Transplantation of M
Background: Enterovirus D68 (EV-D68) is a prominent non-polio enterovirus known to cause severe respiratory infections and poliomyelitis-like illnesses in children. Recently, we identified MFSD6 as a receptor for EV-D68, providing a potential target for blocking viral entry into cells. This study aimed to develop an MFSD6-based decoy receptor to neutralise EV-D68 and elucidate its mechanism of action.
View Article and Find Full Text PDFCurcumin Inhibits HIV-1 by Modulating FOXP3 and Suppressing CCR5 via PI3K/AKT and JAK/STAT Pathways.
J Virol Methods
September 2025
Department of Pathogenic Organism Biology, Henan University of Chinese Medicine, Zhengzhou, Henan, China. Electronic address:
Despite advances in antiretroviral therapy, HIV-1 persistence and immune dysregulation remain unresolved challenges. Here, we demonstrate that curcumin, a low-toxicity natural compound, can inhibit HIV-1 through simultaneous inhibition of the PI3K/AKT and JAK/STAT pathways, leading to downregulation of the viral co-receptor CCR5 and the immune checkpoint transcription factor FOXP3. Using CHIP and EMSA experiments, we found that curcumin disrupts the binding of FOXP3 to the CCR5 promoter, thereby reducing viral entry.
View Article and Find Full Text PDFAttenuate host susceptibility to respiratory virus invasion by inhibiting interactions between host proteins SLC16A3 and AP1G1.
Microbiol Spectr
September 2025
Institute of Chinese Materia Medica, China Academy of Chinese Medical Sciences, Beijing, China.
Modulating cell endocytosis activity to reduce host susceptibility to virus represents a promising strategy for antiviral drug development. In this study, we reveal that lactate transporter SLC16A3 is a critical host factor for reducing diverse virus invasion. By performing metabolomics, proteomics, and thermal proteome profiling experiments, AP1G1, a pivotal protein involved in cellular endocytosis, was indiscriminately screened as a chaperone of SLC16A3.
View Article and Find Full Text PDF