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Global post-translational modification profiling of HIV-1-infected cells reveals mechanisms of host cellular pathway remodeling
- Johnson, Jeffrey R;
- Crosby, David C;
- Hultquist, Judd F;
- Kurland, Andrew P;
- Adhikary, Prithy;
- Li, Donna;
- Marlett, John;
- Swann, Justine;
- Hüttenhain, Ruth;
- Verschueren, Erik;
- Johnson, Tasha L;
- Newton, Billy W;
- Shales, Michael;
- Simon, Viviana A;
- Beltrao, Pedro;
- Frankel, Alan D;
- Marson, Alexander;
- Cox, Jeffery S;
- Fregoso, Oliver I;
- Young, John AT;
- Krogan, Nevan J
- et al.
Published Web Location
https://doi.org/10.1016/j.celrep.2022.110690Abstract
Viruses must effectively remodel host cellular pathways to replicate and evade immune defenses, and they must do so with limited genomic coding capacity. Targeting post-translational modification (PTM) pathways provides a mechanism by which viruses can broadly and rapidly transform a hostile host environment into a hospitable one. We use mass spectrometry-based proteomics to quantify changes in protein abundance and two PTM types-phosphorylation and ubiquitination-in response to HIV-1 infection with viruses harboring targeted deletions of a subset of HIV-1 genes. PTM analysis reveals a requirement for Aurora kinase activity in HIV-1 infection and identified putative substrates of a phosphatase that is degraded during infection. Finally, we demonstrate that the HIV-1 Vpr protein inhibits histone H1 ubiquitination, leading to defects in DNA repair.
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