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Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

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Isolation, Transfection, and Culture of Primary Human Monocytes
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HIV-1 transforms the monocyte plasma membrane proteome.

Irena Kadiu1, Tong Wang, Joshua D Schlautman

  • 1Department of Pharmacology and Experimental Neuroscience, Center for Neurovirology and Neurodegenerative Disorders, University of Nebraska Medical Center, Omaha, NE 68198-5880, USA.

Cellular Immunology
|April 11, 2009
PubMed
Summary

Human immunodeficiency virus type 1 (HIV-1) alters monocyte proteomes, causing protein translocation to the plasma membrane. This leads to cellular activation, oxidative stress, and programmed cell death (apoptosis).

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Area of Science:

  • Immunology
  • Cell Biology
  • Virology

Background:

  • The impact of HIV-1 on monocyte proteome is not fully understood.
  • HIV-1 exposure may induce protein translocation from the cytosol to the plasma membrane.

Purpose of the Study:

  • To investigate HIV-1-induced changes in the monocyte proteome.
  • To determine the functional consequences of these proteomic alterations, focusing on protein translocation and cell death pathways.

Main Methods:

  • Cell surface labeling with CyDye fluorophores.
  • Two-dimensional differential in-gel electrophoresis (2D DIGE).
  • Liquid chromatography tandem mass spectrometry (LC-MS/MS).

Main Results:

  • Fifty-three percent of HIV-1-induced proteins were associated with the plasma membrane.
  • These proteins were linked to cellular activation and oxidative stress, including biliverdin reductase and heat shock protein 70.
  • HIV-1 induced protein translocation correlated with cathepsin B-, caspase 9-, and caspase 3-dependent apoptosis.
  • Phorbol 12-myristate 13-acetate (PMA)-treated monocytes underwent cathepsin B-dependent necrosis, bypassing caspase pathways.

Conclusions:

  • HIV-1 uniquely modulates monocyte activation and oxidative stress.
  • These changes are linked to stress-induced cell death but do not influence viral infection dynamics.