期刊
CELL REPORTS
卷 33, 期 1, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.celrep.2020.108235
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资金
- Wellcome Trust PhD studentships
- Sir Henry Dale Fellowship - Wellcome Trust [098406/Z/12/B]
- Sir Henry Dale Fellowship - Royal Society [098406/Z/12/B]
- Wellcome Trust Senior Clinical Research Fellowship [108070/Z/15/Z]
- Biotechnology and Biological Sciences Research Council (BBSRC) Research Grant [BB/M021424/1]
- Cambridge NIHR BRC Cell Phenotyping Hub
- BBSRC [BB/M021424/1] Funding Source: UKRI
- Wellcome Trust [098406/Z/12/B] Funding Source: Wellcome Trust
Herpesviruses are ubiquitous in the human population and they extensively remodel the cellular environment during infection. Multiplexed quantitative proteomic analysis over the time course of herpes simplex virus 1 (HSV-1) infection was used to characterize changes in the host-cell proteome and the kinetics of viral protein production. Several host-cell proteins are targeted for rapid degradation by HSV-1, including the cellular trafficking factor Golgi-associated PDZ and coiled-coil motif-containing protein (GOPC). We show that the poorly characterized HSV-1 pUL56 directly binds GOPC, stimulating its ubiquitination and proteasomal degradation. Plasma membrane profiling reveals that pUL56 mediates specific changes to the cell-surface proteome of infected cells, including loss of interleukin-18 (IL18) receptor and Toll-like receptor 2 (TLR2), and that cell-surface expression of TLR2 is GOPC dependent. Our study provides significant resources for future investigation of HSV-host interactions and highlights an efficient mechanism whereby a single virus protein targets a cellular trafficking factor to modify the surface of infected cells.
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