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The protein pattern of PMF virus, a type-D retrovirus from malignant permanent human cell lines
Abstract:
The protein pattern of a type-D retrovirus (PMFV) isolated from and propagated in human cell lines has been investigated using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Staining with Coomassie blue and labeling with 14C-leucine/14C-lysine revealed five viral polypeptides with molecular weights of 10,000, 12,000, 15,000, 25,000, and 68,000. The 68,000 D-protein was shown to be a glycoprotein by incorporation of 3H-glucosamine and the 15,000 D-protein was identified as a phosphoprotein. By comparing PMFV with the closely related Mason-Pfizer monkey virus (MPMV) in co-electrophoresis experiments no clear difference was detected in viral 14C-leucine/14C-lysine profiles. The viruses differ, however, with respect to their glycoprotein patterns. A glycoprotein corresponding to the gp20 of MPMV has not been detected in PMFV irrespective of the cell line used for propagation of viruses.
Insights
This study analyzed the protein profile of a type-D retrovirus (PMFV) using SDS-PAGE, identifying five key viral polypeptides. PMFV shares similarities with MPMV but differs in its glycoprotein patterns.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Type-D retroviruses are significant in virological research.
- Understanding viral protein composition is crucial for characterizing retroviruses.
- Human cell lines provide a model for studying virus propagation and protein expression.
Purpose of the Study:
- To investigate the protein pattern of a type-D retrovirus (PMFV) isolated from human cell lines.
- To compare the protein profile of PMFV with the closely related Mason-Pfizer monkey virus (MPMV).
- To identify specific viral proteins, including glycoproteins and phosphoproteins.
Main Methods:
- Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was employed for protein separation.
- Coomassie blue staining and radiolabeling with 14C-leucine/14C-lysine were used to visualize and quantify viral polypeptides.
- Incorporation of 3H-glucosamine identified glycoproteins.
- Co-electrophoresis was performed to compare PMFV and MPMV.
Main Results:
- Five viral polypeptides were identified in PMFV with molecular weights of 10,000, 12,000, 15,000, 25,000, and 68,000.
- The 68,000 D-protein was confirmed as a glycoprotein, and the 15,000 D-protein as a phosphoprotein.
- PMFV and MPMV showed similar 14C-leucine/14C-lysine profiles.
- Significant differences were observed in the glycoprotein patterns between PMFV and MPMV, with a specific gp20-like glycoprotein absent in PMFV.
Conclusions:
- PMFV possesses a distinct protein composition, including specific glycoproteins and phosphoproteins.
- Comparative analysis reveals both conserved and divergent features between PMFV and MPMV, particularly in glycosylation patterns.
- These findings contribute to the molecular characterization of type-D retroviruses and their relationship to MPMV.