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Structural proteins of Herpesvirus saimiri
Journal of Virology
|September 1, 1983
Summary
Herpesvirus saimiri virions contain 21 proteins, including glycoproteins and phosphoproteins. Strain-specific protein differences were minor, suggesting DNA sequence is a better taxonomic marker than protein architecture for distinguishing H. saimiri strains.
Area of Science:
- Virology
- Molecular Biology
- Biochemistry
Background:
- Herpesvirus saimiri (H. saimiri) is a widely studied oncogenic herpesvirus.
- Understanding the structural components of H. saimiri virions is crucial for comprehending its biology and pathogenesis.
Purpose of the Study:
- To characterize the polypeptide composition of purified Herpesvirus saimiri particles.
- To identify and differentiate viral proteins, including glycoproteins, phosphoproteins, and other polypeptides.
- To compare the protein architecture across different H. saimiri strains and assess its utility as a taxonomic criterion.
Main Methods:
- Purification of Herpesvirus saimiri particles from infected owl monkey kidney cell cultures.
- Analysis of virion polypeptides using polyacrylamide gel electrophoresis (PAGE).
- Identification of proteins via Coomassie blue staining and [35S]methionine labeling followed by autoradiography.
- Precipitation of viral proteins using immune sera to confirm virion association.
- Analysis of protein profiles from different H. saimiri strains.
Main Results:
- A total of 21 predominant polypeptides were identified in H. saimiri virions, ranging from 12,000 to 160,000 daltons.
- Four glycoproteins (gp 155/160, gp 128, gp 84/90, gp 55) and three non-glycosylated polypeptides (p71, p35, p28) were localized to the envelope or matrix.
- The nucleocapsid fraction contained at least four phosphoproteins (pp132, pp118, pp55, pp13) and ten unmodified polypeptides.
- Most viral proteins, including all glycoproteins, showed conserved migration patterns across different H. saimiri strains.
- Strain-specific size variations were observed in three of the four phosphoproteins.
- Overall protein architecture similarity contrasts with biological variability, such as oncogenic potential.
Conclusions:
- The study provides a detailed characterization of the Herpesvirus saimiri virion proteome.
- Protein composition is largely conserved among H. saimiri strains, limiting its use for taxonomic distinction.
- DNA sequence divergence is a more reliable criterion for differentiating H. saimiri strains than virion protein analysis.