Dataset Information

Cross-linking MS analysis of HIV-2 Vpx-PHD3 protein interaction

ABSTRACT: This dataset presents chemical crosslinking mass spectrometry (CL-MS) analysis of protein-protein interactions between HIV-2 Vpx and PHD3. The experimental data includes MS spectra obtained from protein complexes comprising recombinant Vpx and PHD3 crosslinked using DSBU under physiological conditions. The samples underwent tryptic digestion following standard proteomics protocols, and the resulting peptides were analyzed using high-resolution LC-MS/MS.

ORGANISM(S): Human Immunodeficiency Virus 2

SUBMITTER: Kei Miyakawa

PROVIDER: PXD059241 | JPOST Repository | Thu Apr 03 00:00:00 BST 2025

REPOSITORIES: jPOST

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	200714HF_Vx93_3_in-sol_150min.mgf	Mgf
	200714HF_Vx93_3_in-sol_150min.mzid	Mzid
	200714HF_Vx93_3_in-sol_150min.raw	Raw
	200714HF_Vx93_3_in-sol_150min.xlsx	Xlsx
	Vx93_recombinant_v20200622.fasta	Fasta

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Publications

PHD3-VHL axis controls HIV-2 infection through oxygen-dependent hydroxylation and degradation of Vpx.

Miyakawa Kei K Tanaka Kiho K Ino Yoko Y Kimura Yayoi Y Kameya Taichi T Mizukoshi Fuminori F Nishi Mayuko M Yokoyama Masaru M Nakabayashi Jun J Nomaguchi Masako M Sato Hironori H Kimura Hirokazu H Akari Hirofumi H Miura Tomoyuki T Takaoka Akinori A Hasegawa Hideki H Matano Tetsuro T Minamishima Yoji Andrew YA Ryo Akihide A

PLoS pathogens 20250616 6

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]

PMID: 40522994

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