Add reference HIV-1 incorporates a large array of host proteins into virions. Determining the host protein composition in HIV virions has technical difficulties, including co-purification of microvesicles. We developed an alternative purification technique using cholesterol that differentially modulates the density of virions and microvesicles (density modification, DM) allowing for high-yield virion purification that is essential for tandem mass spectrometric and quantitative proteomic (iTRAQ) analysis. DM purified virions were analyzed using iTRAQ and validated against Optiprep (60% iodixanol) purified virions. We were able to characterize host protein incorporation in DM-purified HIV particles derived from CD4+ T cell lines; we compared this dataset to a reprocessed dataset of monocyte-derived macrophages (MDM) derived HIV-1 searched using PrpArML which uses multiple search algorithms (OMSSA, X!Tandem with native, k-score and s-score scoring, MASCOT, MyriMatch, and InSpecT ). The database used for search was the UniProt-SwissProt database (version 2010.11.02; 522,019 sequences). Peptides were combined on PepARML using a random forest approach (Weka) and the results were then parsed into MASPECTRAS 2 with minimum two peptide for a protein and a spectrum false discovery rate of 5%. Peptides assigned  to keratin were excluded, and since the analysis was focused on host proteins, viral peptide assignments were excluded. Protein redundancy was removed by MS based evidence clustering. Link to the paper related to the reprocessed MDM dataset: PMID: 16940516, the dataset itself is not publicly available.