Identification of ribosome-associated viral and cellular basic proteins during the course of infection with herpes simplex virus type 1

Autor: Greco, A., Bienvenut, W., Sanchez, J. C., Kindbeiter, K., Hochstrasser, D., Madjar, J. J., Diaz, J. J.
Přispěvatelé: Centre de génétique et de physiologie moléculaire et cellulaire (CGPhiMC), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2001
Předmět:
Zdroj: Proteomics
Proteomics, Wiley-VCH Verlag, 2001, 1 (4), pp.545-9. ⟨10.1002/1615-9861(200104)1:43.0.CO;2-G⟩
ISSN: 1615-9853
1615-9861
DOI: 10.1002/1615-9861(200104)1:43.0.CO;2-G⟩
Popis: 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.
Databáze: OpenAIRE
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