Characterization of histone post-translational modifications during virus infection using mass spectrometry-based proteomics

Methods. 2015 Nov 15:90:8-20. doi: 10.1016/j.ymeth.2015.06.008. Epub 2015 Jun 17.

Abstract

Viruses are obligate intracellular parasites that necessarily rely on hijacking cellular resources to produce viral progeny. The success of viral infection requires manipulation of host chromatin in order to activate genes useful for production of viral proteins as well as to suppress antiviral responses. Host chromatin manipulation on a global level is likely reliant on modulation of post-translational modifications (PTMs) on histone proteins. Mass spectrometry (MS) is a powerful tool to quantify and identify novel histone PTMs, beyond the limitations of site-specific antibodies. Here, we employ MS to investigate global changes in histone PTM relative abundance in human cells during infection with adenovirus. Our method reveals several changes in histone PTM patterns during infection. We propose that this method can be used to uncover global changes in histone PTM patterns that are universally modulated by viruses to take over the cell.

Keywords: Epigenetics; Histone; Mass spectrometry; Pathogen; Post-translational modifications; Proteomics; Virus.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenoviruses, Human / genetics*
  • Adenoviruses, Human / pathogenicity
  • Histones / metabolism*
  • Humans
  • Mass Spectrometry / methods*
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Proteomics / methods*
  • Viral Proteins / metabolism*

Substances

  • Histones
  • Viral Proteins