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Phosphorylation of ribosomal protein L30 after herpes simplex virus type 1 infection
D Simonin1, J J Diaz, K Kindbeiter
1CNRS UMR 30, Faculté de Médecine, Lyon, France.
Abstract:
In addition to an irreversible stimulation of S6 ribosomal protein phosphorylation, there is a modification of a subset of ribosomal proteins by phosphorylation after herpes simplex virus type 1 (HSV-1) infection. Moreover, in the course of this infection, three additional phosphorylated proteins can be extracted from ribosomes and separated by two-dimensional electrophoresis (2-DE) of total ribosomal proteins. One of them exhibits an identical molecular mass to L30, while being more acidic. This protein is phosphorylated on serine residues. The kinetics of appearance of this protein in the ribosomal fraction correlated with a decrease in L30 staining, as shown by 2-DE. Determination of the N-terminal amino acid sequence of this extra phosphoprotein and of L30-derived peptides demonstrated the identity of these two proteins.
Insights
Herpes simplex virus type 1 (HSV-1) infection alters ribosomal protein phosphorylation. A novel phosphorylated protein, identical to ribosomal protein L30, appears during infection, indicating a role for HSV-1 in regulating protein synthesis.
Area of Science:
- Molecular Virology
- Cellular Biology
- Protein Biochemistry
Background:
- Herpes simplex virus type 1 (HSV-1) infection is known to induce changes in host cell processes.
- Ribosomal protein phosphorylation is a key regulatory mechanism in protein synthesis.
- Previous studies indicated HSV-1 infection causes irreversible S6 ribosomal protein phosphorylation.
Purpose of the Study:
- To investigate the comprehensive impact of HSV-1 infection on ribosomal protein phosphorylation.
- To identify and characterize novel phosphorylated proteins associated with ribosomes during HSV-1 infection.
- To elucidate the relationship between the identified phosphoprotein and known ribosomal proteins.
Main Methods:
- Herpes simplex virus type 1 (HSV-1) infection of host cells.
- Extraction and separation of total ribosomal proteins using two-dimensional electrophoresis (2-DE).
- Analysis of protein phosphorylation patterns, molecular mass, acidity, and N-terminal amino acid sequencing.
Main Results:
- HSV-1 infection leads to the phosphorylation of a subset of ribosomal proteins, beyond S6.
- Three additional phosphorylated proteins were identified in the ribosomal fraction post-infection.
- One novel phosphoprotein was found to be more acidic than ribosomal protein L30 but shared its molecular mass and N-terminal sequence, indicating it is a modified form of L30.
Conclusions:
- HSV-1 infection induces significant alterations in ribosomal protein phosphorylation.
- A modified, phosphorylated form of ribosomal protein L30 is generated during HSV-1 infection.
- This finding suggests a potential mechanism by which HSV-1 may regulate host protein synthesis.