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Methylation of the polyomavirus major capsid protein VP1

K S Burton1, R A Consigli

  • 1Division of Biology, Kansas State University, Manhattan 66506, USA.

Virus Research
|February 1, 1996
PubMed

Insights

Polyomavirus VP1, a major capsid protein, undergoes methylation. This modification involves trimethyllysine and monomethylarginine, expanding our understanding of viral protein regulation.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • The major capsid protein of Polyomavirus, VP1, is known to be modified by phosphorylation, sulfation, acetylation, and hydroxylation.
  • These post-translational modifications play crucial roles in viral replication and assembly.

Purpose of the Study:

  • To investigate whether Polyomavirus VP1 is subject to methylation.
  • To identify the specific methylated amino acid residues on VP1.

Main Methods:

  • Infected cell cultures were treated with cycloheximide and [3H-methyl]-L-methionine.
  • VP1 was immunoprecipitated, followed by SDS-PAGE and fluorography to detect methylation.
  • Amino acid analysis of labeled VP1 was performed using two-dimensional paper chromatography and HPLC.

Main Results:

  • Methylation was confirmed to occur on the Polyomavirus VP1 protein.
  • Analysis revealed the presence of 3H-labeled trimethyllysine and monomethylarginine on VP1.

Conclusions:

  • Polyomavirus VP1 is a methylated protein, adding to its known post-translational modifications.
  • The identification of trimethyllysine and monomethylarginine provides specific insights into the methylation sites on VP1.

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