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Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1
- Source :
- PROTEOMICS. 1:545-549
- Publication Year :
- 2001
- Publisher :
- Wiley, 2001.
-
Abstract
- Herpes simplex virus type 1 (HSV-1) infection induces severe alterations of the translational apparatus, including the phosphorylation of a few ribosomal proteins, and the progressive association of several nonribosomal proteins to ribosomes. Therefore, we hypothesized that ribosomes themselves could contribute to the HSV-1-induced translational control of host and viral gene expression. As a prerequisite to test this hypothesis, we undertook the identification of the nonribosomal proteins associated to the ribosomes during the course of HSV-1 infection. After separation by two-dimensional polyacrylamide gel electrophoresis of basic proteins extracted from the ribosomal fraction, the identification of unknown protein spots was carried out by N-terminal sequencing and peptide mass determination by mass spectrometry. This allowed us to identify HSV-1 VP19C and VP26 that associated to ribosomes with different kinetics. Another nonribosomal protein turned out to be the poly(A)-binding protein 1 (PAB1P). Newly synthesized PAB1P continued to associate to ribosomes all along infection.
Details
- ISSN :
- 16159861 and 16159853
- Volume :
- 1
- Database :
- OpenAIRE
- Journal :
- PROTEOMICS
- Accession number :
- edsair.doi...........4823f6b2ccceec4308e0352e7ddeb768