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J Proteome Res. 2015 May 1;14(5):2121-42. doi: 10.1021/pr5012284. Epub 2015 Apr 15.

Quantification of the host response proteome after herpes simplex virus type 1 infection.

Author information

1
†Department of Medical Microbiology, Faculty of Medicine, University of Manitoba, Winnipeg, Manitoba, Canada R3E 0J9.
2
‡Manitoba Center for Proteomics and Systems Biology, University of Manitoba, Room 799 John Buhler Research Centre, Winnipeg, Manitoba, Canada R3E 3P4.
3
§Manitoba Institute of Child Health, University of Manitoba, Room 641 John Buhler Research Centre, Winnipeg, Manitoba, Canada R3E 3P4.
4
∥National Microbiology Laboratory, Public Health Agency of Canada, 1015 Arlington Street, Winnipeg, Manitoba, Canada R3E 3P6.

Abstract

Viruses employ numerous host cell metabolic functions to propagate and manage to evade the host immune system. For herpes simplex virus type 1 (HSV1), a virus that has evolved to efficiently infect humans without seriously harming the host in most cases, the virus-host interaction is specifically interesting. This interaction can be best characterized by studying the proteomic changes that occur in the host during infection. Previous studies have been successful at identifying numerous host proteins that play important roles in HSV infection; however, there is still much that we do not know. This study identifies host metabolic functions and proteins that play roles in HSV infection, using global quantitative stable isotope labeling by amino acids in cell culture (SILAC) proteomic profiling of the host cell combined with LC-MS/MS. We showed differential proteins during early, mid and late infection, using both cytosolic and nuclear fractions. We identified hundreds of differentially regulated proteins involved in fundamental cellular functions, including gene expression, DNA replication, inflammatory response, cell movement, cell death, and RNA post-transcriptional modification. Novel differentially regulated proteins in HSV infections include some previously identified in other virus systems, as well as fusion protein, involved in malignant liposarcoma (FUS) and hypoxia up-regulated 1 protein precursor (HYOU1), which have not been identified previously in any virus infection.

KEYWORDS:

LC−MS/MS; SILAC; cell proteomics; herpes virus; host proteomics; virus−host interactions

PMID:
25815715
DOI:
10.1021/pr5012284
[Indexed for MEDLINE]
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