Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.

Human cytomegalovirus (HCMV) US2, US3, US6 and US11 act in concert to prevent immune recognition of virally infected cells by CD8+ T-lymphocytes through downregulation of MHC class I molecules (MHC-I). Here we show that US2 function goes far beyond MHC-I degradation. A systematic proteomic study usi...

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Main Authors: Jye-Lin Hsu, Dick J H van den Boomen, Peter Tomasec, Michael P Weekes, Robin Antrobus, Richard J Stanton, Eva Ruckova, Daniel Sugrue, Gavin S Wilkie, Andrew J Davison, Gavin W G Wilkinson, Paul J Lehner
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-04-01
Series:PLoS Pathogens
Online Access:https://doi.org/10.1371/journal.ppat.1004811
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author Jye-Lin Hsu
Dick J H van den Boomen
Peter Tomasec
Michael P Weekes
Robin Antrobus
Richard J Stanton
Eva Ruckova
Daniel Sugrue
Gavin S Wilkie
Andrew J Davison
Gavin W G Wilkinson
Paul J Lehner
author_facet Jye-Lin Hsu
Dick J H van den Boomen
Peter Tomasec
Michael P Weekes
Robin Antrobus
Richard J Stanton
Eva Ruckova
Daniel Sugrue
Gavin S Wilkie
Andrew J Davison
Gavin W G Wilkinson
Paul J Lehner
author_sort Jye-Lin Hsu
collection DOAJ
description Human cytomegalovirus (HCMV) US2, US3, US6 and US11 act in concert to prevent immune recognition of virally infected cells by CD8+ T-lymphocytes through downregulation of MHC class I molecules (MHC-I). Here we show that US2 function goes far beyond MHC-I degradation. A systematic proteomic study using Plasma Membrane Profiling revealed US2 was unique in downregulating additional cellular targets, including: five distinct integrin α-chains, CD112, the interleukin-12 receptor, PTPRJ and thrombomodulin. US2 recruited the cellular E3 ligase TRC8 to direct the proteasomal degradation of all its targets, reminiscent of its degradation of MHC-I. Whereas integrin α-chains were selectively degraded, their integrin β1 binding partner accumulated in the ER. Consequently integrin signaling, cell adhesion and migration were strongly suppressed. US2 was necessary and sufficient for degradation of the majority of its substrates, but remarkably, the HCMV NK cell evasion function UL141 requisitioned US2 to enhance downregulation of the NK cell ligand CD112. UL141 retained CD112 in the ER from where US2 promoted its TRC8-dependent retrotranslocation and degradation. These findings redefine US2 as a multifunctional degradation hub which, through recruitment of the cellular E3 ligase TRC8, modulates diverse immune pathways involved in antigen presentation, NK cell activation, migration and coagulation; and highlight US2's impact on HCMV pathogenesis.
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spelling doaj-art-d057a00df10f4bbdb235d95e59e2cbce2025-08-20T02:34:10ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742015-04-01114e100481110.1371/journal.ppat.1004811Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.Jye-Lin HsuDick J H van den BoomenPeter TomasecMichael P WeekesRobin AntrobusRichard J StantonEva RuckovaDaniel SugrueGavin S WilkieAndrew J DavisonGavin W G WilkinsonPaul J LehnerHuman cytomegalovirus (HCMV) US2, US3, US6 and US11 act in concert to prevent immune recognition of virally infected cells by CD8+ T-lymphocytes through downregulation of MHC class I molecules (MHC-I). Here we show that US2 function goes far beyond MHC-I degradation. A systematic proteomic study using Plasma Membrane Profiling revealed US2 was unique in downregulating additional cellular targets, including: five distinct integrin α-chains, CD112, the interleukin-12 receptor, PTPRJ and thrombomodulin. US2 recruited the cellular E3 ligase TRC8 to direct the proteasomal degradation of all its targets, reminiscent of its degradation of MHC-I. Whereas integrin α-chains were selectively degraded, their integrin β1 binding partner accumulated in the ER. Consequently integrin signaling, cell adhesion and migration were strongly suppressed. US2 was necessary and sufficient for degradation of the majority of its substrates, but remarkably, the HCMV NK cell evasion function UL141 requisitioned US2 to enhance downregulation of the NK cell ligand CD112. UL141 retained CD112 in the ER from where US2 promoted its TRC8-dependent retrotranslocation and degradation. These findings redefine US2 as a multifunctional degradation hub which, through recruitment of the cellular E3 ligase TRC8, modulates diverse immune pathways involved in antigen presentation, NK cell activation, migration and coagulation; and highlight US2's impact on HCMV pathogenesis.https://doi.org/10.1371/journal.ppat.1004811
spellingShingle Jye-Lin Hsu
Dick J H van den Boomen
Peter Tomasec
Michael P Weekes
Robin Antrobus
Richard J Stanton
Eva Ruckova
Daniel Sugrue
Gavin S Wilkie
Andrew J Davison
Gavin W G Wilkinson
Paul J Lehner
Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
PLoS Pathogens
title Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
title_full Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
title_fullStr Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
title_full_unstemmed Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
title_short Plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by HCMV US2 in cooperation with UL141.
title_sort plasma membrane profiling defines an expanded class of cell surface proteins selectively targeted for degradation by hcmv us2 in cooperation with ul141
url https://doi.org/10.1371/journal.ppat.1004811
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