Quantitative nuclear proteomics reveals new phenotypes altered in lymphoblastoid cells
Paul Brennan1, Angharad M Shore2, Mathew Clement2
1Department of Medical Biochemistry and Immunology, School of Medicine, Cardiff University, Heath Park, Cardiff, UK. brennanp@cardiff.ac.uk.
Proteomics. Clinical Applications
|August 5, 2015
Summary
Epstein-Barr virus (EBV) infection alters B-lymphocyte proteomes, impacting cell size and function. This study identified key proteins involved in EBV-driven cell immortalization and cancer development.
Area of Science:
- Immunology
- Molecular Biology
- Proteomics
Background:
- B-lymphocytes are crucial for antibody production and are the origin of most human lymphomas.
- Epstein-Barr virus (EBV) immortalizes B-lymphocytes, contributing to cancers and causing significant cellular changes.
Purpose of the Study:
- To compare the proteomes of EBV-negative and EBV-positive B-cell lines from the same individual.
- To identify differentially expressed proteins associated with EBV-induced B-cell activation and immortalization.
Main Methods:
- Utilized isobaric tags for quantitative proteomics.
- Employed Liquid Chromatography-MALDI TOF-TOF mass spectrometry.
- Incorporated subcellular fractionation (detergent and nuclear extracts) for comprehensive protein analysis.
Main Results:
- Quantified 499 proteins in total across B-cell lines.
- Identified 34 differentially expressed proteins in whole cell lysates and 29 in nuclear extracts.
- Subcellular fractionation revealed distinct protein sets, with only four shared between extracts, highlighting its importance.
Conclusions:
- Identified proteins linked to cytoskeletal changes and enhanced antigen recognition in EBV-immortalized cells.
- Discovered novel transcription regulators and ribonuclear proteins potentially driving increased cell size and immortalization.
- Findings offer insights into EBV's role in B-cell lymphomagenesis and cancer progression.
