Nobre, Luis V., Nightingale, Katie, Ravenhill, Benjamin J., Antrobus, Robin, Soday, Lior, Nichols, Jenna, Davies, James ![]() ![]() ![]() ![]() |
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Abstract
Human cytomegalovirus (HCMV) extensively modulates host cells, downregulating >900 human proteins during viral replication and degrading ≥133 proteins shortly after infection. The mechanism of degradation of most host proteins remains unresolved, and the functions of many viral proteins are incompletely characterised. We performed a mass spectrometry-based interactome analysis of 169 tagged, stably-expressed canonical strain Merlin HCMV proteins, and two non-canonical HCMV proteins, in infected cells. This identified a network of >3,400 virus-host and >150 virus-virus protein interactions, providing insights into functions for multiple viral genes. Domain analysis predicted binding of the viral UL25 protein to SH3 domains of NCK Adaptor Protein-1. Viral interacting proteins were identified for 31/133 degraded host targets. Finally, the uncharacterised, non-canonical ORFL147C protein was found to interact with elements of the mRNA splicing machinery, and a mutational study suggested its importance in viral replication. The interactome data will be important for future studies of herpesvirus infection.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Medicine Systems Immunity Research Institute (SIURI) |
Publisher: | eLife Sciences Publications |
ISSN: | 2050-084X |
Funders: | Medical Research Council, Wellcome Trust |
Date of First Compliant Deposit: | 7 January 2020 |
Date of Acceptance: | 24 December 2019 |
Last Modified: | 07 Nov 2023 23:42 |
URI: | https://orca.cardiff.ac.uk/id/eprint/128215 |
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