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Related Experiment Video

Updated: Jun 30, 2025

Live Imaging and Quantification of Viral Infection in K18 hACE2 Transgenic Mice Using Reporter-Expressing Recombinant SARS-CoV-2

Live Imaging and Quantification of Viral Infection in K18 hACE2 Transgenic Mice Using Reporter-Expressing Recombinant SARS-CoV-2

Published on: November 5, 2021

SARS-CoV-2 and UPS with potentials for therapeutic interventions.

Jannatul Ferdoush¹, Rizwaan Abdul Kadir¹, Selin Simay Kaplanoglu¹

¹Department of Biology, Geology, and Environmental Science, University of Tennessee at Chattanooga 615 McCallie Ave, Chattanooga, TN 37403, USA.

|March 15, 2024

Summary

The Ubiquitin Proteasome System (UPS) is crucial for cellular functions and is manipulated by SARS-CoV-2. Targeting UPS components offers potential COVID-19 treatments.

Keywords:

Nsp12 ORF3a ORF7a ORF8 ORF9b PLpro SARS-CoV-2 UPS

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Area of Science:

Molecular Biology
Virology
Immunology

Background:

The Ubiquitin Proteasome System (UPS) regulates essential cellular processes, including protein stability, immune responses, and viral replication.
Viruses, including SARS-CoV-2, can exploit the host UPS for their own replication and pathogenesis, while hosts may use UPS to combat viral infections.

Approach:

This review examines the complex interplay between SARS-CoV-2 and the host UPS.
It analyzes how viral proteins interact with UPS machinery to influence host immune signaling and apoptosis.
Proteomic studies revealing these alterations are highlighted as crucial for identifying therapeutic targets.

Key Points:

SARS-CoV-2 proteins (ORF3a, ORF6, ORF7a, ORF9b, ORF10) interact with the host UPS, affecting immune signaling and apoptosis.
The SARS-CoV-2 papain-like protease (PLpro) interferes with the host UPS to promote viral replication and immune evasion.
Proteomic data reveals significant UPS alterations in SARS-CoV-2 infected cells.

Conclusions:

Understanding the SARS-CoV-2 UPS interaction is key to comprehending COVID-19 pathogenesis.
Targeting viral proteins like PLpro or host-viral interactions offers promising therapeutic strategies.
Potential treatments include zinc-ejector drugs for PLpro and heat treatment for nsp12-mediated degradation.