Proteomics of herpes simplex virus infected cell protein 27: association with translation initiation factors
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The herpes simplex virus (HSV) immediate early ICP27 protein plays an essential role in stimulating viral early and late gene expression. ICP27 appears to be multifunctional in that it has been reported to stimulate viral late gene transcription, polyadenylation site usage, and RNA export. We report here on proteomic studies involving immunoprecipitation of ICP27 and mass spectrometric identification of co-precipitated proteins. These studies show an association of ICP27 with the cellular translation initiation factors poly A binding protein (PABP), eukaryotic initiation factor 3 (eIF3), and eukaryotic initiation factor 4G (eIF4G) in infected cells. Immunoprecipitation-western blot studies confirmed these associations. Finally, purified MBP-tagged ICP27 (MBP-27) can interact with eIF3 subunits p47 and p116 in vitro. These results suggest that ICP27 may also play a role in stimulating translation of certain viral and host mRNAs and/or in inhibiting host mRNA translation.
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Components of SWI/SNF and ISWI chromatin-remodeling complexes were coisolated with the single-stranded DNA-binding protein ICP8.
“Interestingly, components of SWI/SNF and ISWI chromatin-remodeling complexes were coisolated with the single-stranded DNA–binding protein ICP8.”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [34]
The Knipe laboratory used affinity purification-mass spectrometry to study virus-host protein complexes containing ICP27 or ICP8 at an early stage of herpes simplex virus 1 infection in human Hep2 cells.
“For example, the Knipe laboratory (34, 35) used AP-MS to study virus-host protein complexes containing the immediate-early proteins ICP27 or ICP8 at an early stage of herpes simplex virus 1 (HSV-1) infection in human Hep2 cells.”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [34]
In HSV-1-infected human epidermoid cells at 6 hpi, ICP27 interacts with eIF3 subunits p47 and p116, eIF4G, and poly-adenylate binding protein, suggesting ICP27 may interfere with viral or host mRNA translation.
“the Knipe group subsequently identified the eukaryotic translation initiation eIF3 subunits p47 and p116, eIF4G, and poly-adenylate binding protein as cellular interactors of the HSV-1 immediate-early protein ICP27 in human epidermoid cells at 6 hpi. These results suggested that ICP27 may interfere with viral or host mRNA translation [36].”
From Proteomic approaches to uncovering virus–host protein interactions during the progression of viral infection (2016) · cites this paper as [36]
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- Authors
- Fontaine-Rodriguez, E. C., Taylor, T. J., Olesky, M., & Knipe, D. M.
- Affiliations
- Harvard University (US)
- Corresponding author
- Knipe, David M.
- ORCID
- Knipe, David M.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 2004-12
- Volume
- 330
- Issue
- 2
- Pages
- 487-492
- ISSN
- 0042-6822 (ISSN-L)
- OpenAlex
- W1983841815
- Cited by
- 83
- References
- 33
- Citations by year
- 2025: 1 · 2024: 3 · 2022: 1 · 2021: 2 · 2020: 2 · 2018: 6 · 2017: 3 · 2016: 3 · 2015: 7 · 2014: 4 · 2013: 1 · 2012: 4
- FWCI
- 2.88
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Virology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (AI-20530, R01AI020530, T32AI007245)
- Topics
- Health Sciences › Medicine › Epidemiology › Herpesvirus Infections and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Health Sciences › Medicine › Epidemiology › Cytomegalovirus and herpesvirus research
- Keywords
- herpes simplex virus, ICP27, viral immediate-early proteins, translation initiation factors, poly(A)-binding protein, eIF3, eIF4G, protein-protein interaction, viral gene expression, viral mRNA translation
- MeSH terms
- Cell Line, Humans, Mass Spectrometry, Blotting, Western, Immediate-Early Proteins, Simplexvirus, Protein Subunits, Protein Interaction Mapping, Poly(A)-Binding Proteins, Eukaryotic Initiation Factor-4G, Eukaryotic Initiation Factor-3, Eukaryotic Initiation Factors, Immunoprecipitation
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