Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteomic profiling and PRM analysis for quantification of heterologous antigens in HIV-1 Gag VLPs

ABSTRACT: In this study, we evaluated HIV-1 Gag Virus Like Particles (VLPs) for the display of heterologous membrane proteins in their native conformation and lipid environment. The overexpressed membrane protein was quantified in the VLPs by LC-MS/MS based PRM analysis.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Michael Ford

LAB HEAD: Michael Ford

PROVIDER: PXD074653 | Pride | 2026-02-20

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	F212738.dat	Other
	F212739.dat	Other
	F212740.dat	Other
	F212741.dat	Other
	MSB70798AA.raw	Raw

Items per page:

1 - 5 of 11

Similar Datasets

Determination of Gag stoichiometry for different production platforms by PRM analysis

Project description:In this work we established an analytical method of characterization for the Gag protein core and clarify the current variability of Gag stoichiometry in HIV-1 VLPs depending on the cell-based production platform, directly determining the number of Gag molecules per VLP in each case. Three Gag peptides have been validated to quantify the number of monomers using parallel reaction monitoring (PRM)

2022-12-07 | PXD021278 | Pride

Characterization of HEK293 secretome by LC-MS/MS

Project description:Characterization of the extracellular environment of produced VLPs and coproduced extracellular vesicles (EVs)by quantitative proteomics approach. Three conditions were studied: non-transfected, transfected with an empty plasmid as control and with a plasmid coding for HIV-1 Gag polyprotein.

2020-09-28 | PXD018114 | Pride

Multiplexed quantitative proteomic analysis of Human Embryonic Kidney 293 (HEK293)

Project description:Study of the changes in the HEK293 proteome when growing without transfection, when transfected with an empty plasmid and when transfected with Gagcoding gene to produce Gag VLPs,

2020-05-15 | PXD014746 | Pride

Collagen-GAG Biocompatibility Tests

Project description:All mRNA was isolated after 8 hours of culture time in each of three culture conditions. (1) TCPS Plate, (2) Collagen-GAG 2 dimensional coated plate and (3) collagen-GAG three dimensional mesh. Keywords: ordered

2004-11-09 | GSE1937 | GEO

N-terminal VP1 truncation favor T=1 norovirus-like particles

Project description:Noroviruses cause immense sporadic gastroenteritis outbreaks worldwide. Upcoming genotypes, which are divided based on VP1 sequence, further enhance this public thread regularly. Self-assembling properties of the human norovirus major capsid protein VP1 are crucial for using virus-like particles (VLPs) for vaccine development. However, there is no vaccine available yet. Here, VLPs from different variants produced in insect cells are characterized in detail using a set of biophysical and structural tools.

2021-01-11 | PXD023182 | Pride

Transcription profiling of human fibroblasts grown on TCPS plates, Collagen-GAG 2 D plate and Collagen-GAG 3D mesh

2008-06-11 | E-GEOD-1937 | biostudies-arrayexpress

Total RNA-seq analysis of WT and Gag chimera HIV-1 virions

Project description:To investigate how the major HIV-1 structural protein Gag packages viral genomes efficiently, we replaced the NC domain of Gag with RNA binding domains from heterologous cellular RNA binding proteins to generate Gag chimeras. We hypothesize that the Gag chimeras that preferentially bind to purine-rich RNA sequences will package viral genomes efficiently. We performed total RNA-seq to identify the RNAs that are packaged by WT Gag and Gag chimeras in HIV-1 virions.

2025-10-15 | GSE275260 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 3

Project description:To investigate how the major HIV-1 structural protein Gag packages viral genomes efficiently, we replaced the NC domain of Gag with RNA binding domains from heterologous cellular RNA binding proteins to generate Gag chimeras. We hypothesize that the Gag chimeras that preferentially bind to purine-rich RNA sequences will package viral genomes efficiently. We performed CLIP-seq to identify the RNA sequences bound by WT Gag and Gag chimeras in cells, at the plasma membrane, and in virions.

2024-11-30 | GSE281424 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 2

Project description:To investigate how the major HIV-1 structural protein Gag packages viral genomes efficiently, we replaced the NC domain of Gag with RNA binding domains from heterologous cellular RNA binding proteins to generate Gag chimeras. We hypothesize that the Gag chimeras that preferentially bind to purine-rich RNA sequences will package viral genomes efficiently. We performed CLIP-seq to identify the RNA sequences bound by WT Gag and Gag chimeras in cells, at the plasma membrane, and in virions.

2024-11-30 | GSE281423 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 1

Project description:To investigate how the major HIV-1 structural protein Gag packages viral genomes efficiently, we replaced the NC domain of Gag with RNA binding domains from heterologous cellular RNA binding proteins to generate Gag chimeras. We hypothesize that the Gag chimeras that preferentially bind to purine-rich RNA sequences will package viral genomes efficiently. We performed CLIP-seq to identify the RNA sequences bound by WT Gag and Gag chimeras in cells, at the plasma membrane, and in virions.

2024-11-30 | GSE281422 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data