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Establishment of Epstein-Barr Virus Growth-transformed Lymphoblastoid Cell Lines

Establishment of Epstein-Barr Virus Growth-transformed Lymphoblastoid Cell Lines

Published on: November 8, 2011

Epstein-Barr Virus LMP1 Modulates the CD63 Interactome.

Mujeeb Cheerathodi¹, Dingani Nkosi¹, Allaura S Cone¹

¹Department of Biomedical Sciences, Florida State University College of Medicine, Tallahassee, FL 32306, USA.

|April 30, 2021

Summary

The CD63 protein

Keywords:

CD63 Epstein-Barr virus Herpesvirus autophagy exosomes extracellular vesicles interactions latent membrane protein 1 mTOR mass spectrometry proteomics signaling tetraspanin

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Tetraspanin CD63 is a cell surface protein involved in protein trafficking and extracellular vesicle (EV) formation.
CD63 plays a role in the trafficking of LMP1 (latent membrane protein 1) to EVs, influencing intracellular signaling pathways.
Understanding the CD63 interactome is crucial for elucidating its role in cellular processes.

Purpose of the Study:

To comprehensively identify proteins interacting with CD63 using BioID and mass spectrometry.
To investigate how LMP1 modulates the CD63 protein interaction network.
To explore the functional implications of these interactions on cellular signaling and trafficking.

Main Methods:

Utilized the BioID proximity labeling method combined with mass spectrometry to map the CD63 interactome.
Performed biological process enrichment analysis on identified protein networks.
Investigated the interaction of LMP1 with CD63 and its associated proteins, including signaling molecules.

Main Results:

Identified a network of 1600 proteins proximal to CD63, enriched in signal transduction, cell communication, and protein transport.
The CD63 interactome included Rab GTPases, SNARE proteins, and sorting nexins.
LMP1 altered the CD63 interactome, shifting enrichment from protein localization to metabolic processes and translation, and revealed interactions with mTOR, Nedd4 L, and PP2A.

Conclusions:

LMP1 significantly modifies the CD63 protein network, impacting cellular processes.
The findings provide insights into the multiprotein complex formation involving CD63, LMP1, mTOR, Nedd4 L, and PP2A.
This study enhances understanding of the molecular mechanisms underlying endocytic trafficking and extracellular vesicle cargo sorting and secretion.