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Structural phosphoproteins associated with measles virus nucleocapsids from persistently infected cells
Abstract:
Measles virus nucleocapsids were labelled with 3H-amino acids and 32P-orthlls (AV+). When analysed by SDS-PAGE, the two major capsid-associated polypeptides (P, mol. wt. 69,000, and NP, mol. wt. 60,000) were shown to be phosphorylated. Subsequent characterization of the phosphorylated polypeptides by acid hydrolysis and high voltage paper electrophoresis showed that serine and threonine were the major phosphorylated amino acid species. The similarities between the peptide phosphorylation patterns obtained in these studies and those reported earlier for the virus phosphoproteins produced in acute infections (Robbins & Bussell, 1979) indicate that major phosphorylative modifications of the capsid proteins are not involvedin measles virus persistence in AV3 cells.
Insights
Measles virus capsid proteins are phosphorylated on serine and threonine. These modifications do not appear to be involved in measles virus persistence in AV3 cells.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- Measles virus is a significant human pathogen.
- Understanding viral protein modifications is crucial for antiviral strategies.
- Phosphorylation plays a key role in regulating viral protein function.
Purpose of the Study:
- To investigate the phosphorylation status of measles virus capsid proteins.
- To determine the role of protein phosphorylation in measles virus persistence.
Main Methods:
- Measles virus nucleocapsids were labeled with 3H-amino acids and 32P-orthophosphate.
- SDS-PAGE was used to analyze capsid-associated polypeptides.
- Acid hydrolysis and high-voltage paper electrophoresis characterized phosphorylated amino acids.
Main Results:
- The two major capsid proteins, P (69 kDa) and NP (60 kDa), were found to be phosphorylated.
- Serine and threonine were identified as the primary phosphorylated amino acid residues.
- Phosphorylation patterns in persistent infections were similar to acute infections.
Conclusions:
- Major phosphorylative modifications of measles virus capsid proteins are not implicated in viral persistence.
- Further research into other post-translational modifications may be warranted for understanding measles virus persistence.