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Post translational modifications in adenovirus type 2.

Sara Bergström Lind1, Konstantin A Artemenko, Lioudmila Elfineh

  • 1Department of Immunology, Genetics and Pathology, Science for Life Laboratory, Rudbeck Laboratory, Uppsala University, SE-751 85 Uppsala, Sweden; Department of Chemistry-BMC, Science for Life Laboratory, Uppsala University, SE-751 24 Uppsala, Sweden.

Virology
|November 12, 2013
PubMed
Summary

This study reveals new post-translational modifications (PTMs) in adenovirus type 2 (Ad2) proteins using advanced mass spectrometry. These findings demonstrate a greater complexity of the Ad2 virion than previously understood.

Keywords:
2-D SDS-PAGEAdenovirus type 2High resolving mass spectrometryPost translational modification analysis

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Area of Science:

  • Virology
  • Proteomics
  • Biochemistry

Background:

  • Adenovirus type 2 (Ad2) is a significant human pathogen.
  • Understanding Ad2 virion complexity is crucial for developing antiviral strategies.
  • Post-translational modifications (PTMs) play a key role in protein function and regulation.

Purpose of the Study:

  • To investigate the Ad2 proteome at the PTM level.
  • To identify novel phosphorylation, nitration, and acetylation sites on Ad2 proteins.
  • To elucidate the functional implications of PTMs on Ad2 structure and behavior.

Main Methods:

  • Combined 2-D SDS-PAGE with liquid chromatography-high resolving mass spectrometry (LC-MS).
  • Employed in-solution and in-gel digestion strategies.
  • Utilized titanium dioxide enrichment for phosphopeptide analysis.
  • Performed manual verification of PTM positions.

Main Results:

  • Identified new phosphorylation sites on pIII, pIIIa, and pIV proteins, explaining observed protein spot trains.
  • pIIIa protein exhibited extensive modification with 18 phosphorylation sites, 3 nitrated tyrosines, and 1 sulfated tyrosine.
  • Nitrated tyrosines were also found in pII; lysine acetylations were detected in pII and pVI.

Conclusions:

  • The Ad2 virion possesses a more intricate proteome than previously recognized.
  • PTMs significantly contribute to the complexity and potential functional diversity of Ad2 proteins.
  • This study provides a foundation for further research into Ad2 PTMs and their impact on viral infectivity.