Related Experiment Video
Updated: Jul 7, 2025
10:22
Isolation of Viral Replication Compartment-enriched Sub-nuclear Fractions from Adenovirus-infected Normal Human Cells
Published on: November 12, 2015
8.8K
Identification of Adenovirus E1B-55K Interaction Partners through a Common Binding Motif
Nafiseh Chalabi Hagkarim1, Wing-Hang Ip2, Luca D Bertzbach2
1Institute for Cancer and Genomic Sciences, The Medical School, University of Birmingham, Birmingham B15 2TT, UK.
Viruses
|December 23, 2023
Summary
Adenovirus E1B-55K protein binds cellular proteins via a specific motif, leading to their degradation. This study identifies new binding partners and clarifies the mechanism of viral protein interactions.
Area of Science:
- Virology
- Molecular Biology
- Protein Biochemistry
Background:
- Adenovirus protein E1B-55K is vital for viral replication.
- E1B-55K forms a complex with E4orf6, acting as a ubiquitin E3 ligase.
- This complex targets cellular proteins for proteasomal degradation.
Purpose of the Study:
- To investigate the binding mechanism of adenovirus E1B-55K protein.
- To identify novel cellular proteins interacting with E1B-55K.
- To understand how E1B-55K influences host protein stability during infection.
Main Methods:
- In silico analysis of protein sequences for potential binding motifs.
- Co-immunoprecipitation assays to detect protein-protein interactions.
- Western blotting to assess protein degradation during viral infection.
Main Results:
- Many cellular proteins, including ATR, CHK1, USP9, and USP34, were found to co-immunoprecipitate with E1B-55K.
- A conserved p53 binding motif (xWxxxPx) was identified in E1B-55K interactors.
- During adenovirus infection, CSB, CHK1, and USP9 were degraded in a cullin-dependent manner, while ATR and USP34 remained stable.
Conclusions:
- The xWxxxPx motif is a key determinant for E1B-55K binding to diverse cellular proteins.
- Adenovirus E1B-55K hijacks the host ubiquitination machinery to degrade specific cellular proteins.
- Protein structure around the motif, not just sequence, dictates binding and subsequent degradation.
