Abstract:
:Proteasomes are critical for the processing of antigens for presentation through the major histocompatibility complex (MHC) class I pathway. HIV-1 Gag protein is a component of several experimental HIV-1 vaccines. Therefore, understanding the processing of HIV-1 Gag protein and the resulting epitope repertoire is essential. Purified proteasomes from mature dendritic cells (DC) and activated CD4(+) T cells from the same volunteer were used to cleave full-length Gag-p24 protein, and the resulting peptide fragments were identified by mass spectrometry. Distinct proteasomal degradation patterns and peptide fragments were unique to either mature DC or activated CD4(+) T cells. Almost half of the peptides generated were cell type specific. Two additional differences were observed in the peptides identified from the two cell types. These were in the HLA-B35-Px epitope and the HLA-B27-KK10 epitope. These epitopes have been linked to HIV-1 disease progression. Our results suggest that the source of generation of precursor MHC class I epitopes may be a critical factor for the induction of relevant epitope-specific cytotoxic T cells.
journal_name
J Viroljournal_title
Journal of virologyauthors
Steers NJ,Currier JR,Kijak GH,di Targiani RC,Saxena A,Marovich MA,Kim JH,Michael NL,Alving CR,Rao Mdoi
10.1128/JVI.01790-10subject
Has Abstractpub_date
2011-02-01 00:00:00pages
1541-53issue
4eissn
0022-538Xissn
1098-5514pii
JVI.01790-10journal_volume
85pub_type
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