Proteomics

Dataset Information

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PHD3-mediated HIV-2 Vpx peptide hydroxylation

ABSTRACT: This dataset contains comparative mass spectrometry analysis investigating proline hydroxylation of synthetic HIV-2 Vpx peptides under two conditions: with and without PHD3 enzyme treatment. The analysis was performed using a high-resolution mass spectrometer coupled to a nano-LC system. The dataset provides comprehensive information about post-translational modifications, focusing on site-specific proline hydroxylation events.

ORGANISM(S): Human Immunodeficiency Virus 2

SUBMITTER: Kei Miyakawa 

PROVIDER: PXD059242 | JPOST Repository | Thu Apr 03 00:00:00 BST 2025

REPOSITORIES: jPOST

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Dataset's files

Source:
Action DRS
191029Elite_Vpx_PHD3_1.raw Raw
191029Elite_Vpx_PHD3_2.raw Raw
191029Elite_Vpx_control_1.raw Raw
191029Elite_Vpx_control_2.raw Raw
191029Elite_Vpx_peptide.csv Csv
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Publications

HIV-2 viral protein X (Vpx) plays a pivotal role in antagonizing the host restriction factors, including SAMHD1 and components of the HUSH complex, to facilitate viral replication. However, the regulatory mechanisms controlling Vpx stability remain unclear. In this study, we identify the von Hippel-Lindau (VHL) tumor suppressor as a novel E3 ubiquitin ligase that specifically targets Vpx for proteasomal degradation. Mechanistically, we demonstrate that VHL-mediated degradation depends on the oxy  ...[more]

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