Viruses, Vol. 13, Pages 675: Epstein-Barr Virus LMP1 Modulates the CD63 Interactome

Viruses, Vol. 13, Pages 675: Epstein-Barr Virus LMP1 Modulates the CD63 Interactome Viruses doi: 10.3390/v13040675 Authors: Mujeeb Cheerathodi Dingani Nkosi Allaura S. Cone Sara B. York David G. Meckes Tetraspanin CD63 is a cluster of cell surface proteins with four transmembrane domains; it is associated with tetraspanin-enriched microdomains and typically localizes to late endosomes and lysosomes. CD63 plays an important role in the cellular trafficking of different proteins, EV cargo sorting, and vesicle formation. We have previously shown that CD63 is important in LMP1 trafficking to EVs, and this also affects LMP1-mediated intracellular signaling including MAPK/ERK, NF-κB, and mTOR activation. Using the BioID method combined with mass spectrometry, we sought to define the broad CD63 interactome and how LMP1 modulates this network of interacting proteins. We identified a total of 1600 total proteins as a network of proximal interacting proteins to CD63. Biological process enrichment analysis revealed significant involvement in signal transduction, cell communication, protein metabolism, and transportation. The CD63-only interactome was enriched in Rab GTPases, SNARE proteins, and sorting nexins, while adding LMP1 into the interactome increased the presence of signaling and ribosomal proteins. Our results showed that LMP1 alters the CD63 interactome, shifting the network of protein enrichment from protein localization and vesicle-mediated transportation to...
Source: Viruses - Category: Virology Authors: Tags: Article Source Type: research
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