Опубликована: Янв. 1, 2024
Язык: Английский
Journal of Clinical Virology Plus, Год журнала: 2025, Номер unknown, С. 100206 - 100206
Опубликована: Янв. 1, 2025
Язык: Английский
Процитировано
0
Journal of Virology, Год журнала: 2025, Номер unknown
Опубликована: Май 27, 2025
ABSTRACT Recombination in RNA viruses contributes to virus evolution and rapid emergence of new viral variants that helps evade host’s antiviral strategies. Host factors play important but poorly characterized roles recombination. The authors expressed Legionella bacterium effector proteins SARS-CoV-2 human metapneumovirus (HMPV) yeast test their effects on tomato bushy stunt (TBSV) identified 16 effectors, six SARS-CoV-2, two HMPV affecting TBSV recombination likely target shared host with TBSV. Among the targets effectors/viral was autophagy pathway. Inhibition by expression RavZ LegA9 effectors reduced production recombinants plants. Induction rapamycin, via nitrogen starvation or overexpression ATG2 lipid transfer protein, led enhanced Using vitro replicase assembly giant unilamellar vesicles confirmed critical role phosphatidylethanolamine We suggest pro-recombination co-opted is provide abundant phospholipids for replication organelle biogenesis. Overall, this work highlights membrane context regulation show N M2-1 enhance protecting RNAs from Xrn1 5´−3´ exoribonuclease yeast. Altogether, novel strategy using as a cellular system sensor might assist identification functional various bacterial IMPORTANCE Positive-strand (+)RNA replicate cytosol infected cells exploiting resources frequently lead diseases. Virus results generation contribute adaptation hosts. proteins, This approach revealed heterologous TBSV, including In replication. nucleocapsid protein are shown Thus, TBSV/yeast can be used find functions proteins.
Язык: Английский
Процитировано
0
Developmental & Comparative Immunology, Год журнала: 2024, Номер unknown, С. 105293 - 105293
Опубликована: Ноя. 1, 2024
Язык: Английский
Процитировано
1
Biochemical Society Transactions, Год журнала: 2024, Номер unknown
Опубликована: Сен. 2, 2024
E3 ubiquitin ligases regulate the composition of proteome. These enzymes mono- or poly-ubiquitinate their substrates, directly altering protein function targeting proteins for degradation by proteasome. In this review, we discuss opposing roles human as effectors and targets in evolutionary battle between host pathogen, specifically context SARS-CoV-2 infection. Through complex effects on transcription, translation, trafficking, can either attenuate infection become vulnerabilities that are exploited virus to suppress host's antiviral defenses. For example, ligase RNF185 regulates stability envelope through ubiquitin-proteasome pathway, depletion significantly increases viral titer (iScience (2023) 26, 106601). We highlight recent advances identify functions numerous life cycle assess potential novel agents.
Язык: Английский
Процитировано
0
Journal of Medical Virology, Год журнала: 2024, Номер 96(9)
Опубликована: Сен. 1, 2024
The ubiquitin-proteasome system is frequently employed to degrade viral proteins, thereby inhibiting replication and pathogenicity. Through an analysis of the degradation kinetics all SARS-CoV-2 our study revealed rapid several particularly NSP5. Additionally, we identified FBXO22, E3 ubiquitin ligase, as primary regulator NSP5 ubiquitination. Moreover, validated interaction between FBXO22 NSP5, demonstrating that FBXO22-mediated ubiquitination facilitated its recognition by proteasome, leading subsequent degradation. Specifically, catalyzed formation K48-linked polyubiquitin chains on at lysine residues 5 90. Knockdown resulted in decreased levels, increased stability, enhanced ability evade host innate immune response. Notably, protein level were negatively correlated with load, highlighting importance replication. This elucidates molecular mechanism which mediates underscores critical role limiting identification a stability provides new insights potential avenues for targeting antiviral strategies.
Язык: Английский
Процитировано
0
Опубликована: Янв. 1, 2024
Язык: Английский
Процитировано
0