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Recognition and eradication of infected cells by cytotoxic T lymphocytes is a key defense mechanism against intracellular pathogens. High-throughput definition of HLA class I-associated immunopeptidomes by mass spectrometry is an increasingly important analytical tool to advance our understanding of the induction of T-cell responses against pathogens such as HIV-1. We utilized a liquid chromatography tandem mass spectrometry workflow including de novo-assisted database searching to define the HLA class I-associated immunopeptidome of HIV-1-infected human cells. We here report for the first time the identification of 75 HIV-1-derived peptides bound to HLA class I complexes that were purified directly from HIV-1-infected human primary CD4(+) T cells and the C8166 human T-cell line. Importantly, one-third of eluted HIV-1 peptides had not been previously known to be presented by HLA class I. Over 82% of the identified sequences originated from viral protein regions for which T-cell responses have previously been reported but for which the precise HLA class I-binding sequences have not yet been defined. These results validate and expand the current knowledge of virus-specific antigenic peptide presentation during HIV-1 infection and provide novel targets for T-cell vaccine development.

Original publication

DOI

10.1002/eji.201545890

Type

Journal article

Journal

Eur J Immunol

Publication Date

01/2016

Volume

46

Pages

60 - 69

Keywords

Cytotoxic T cells, Human immunodeficiency virus type I, Human leukocyte antigen, Immunopeptidome, Mass spectrometry, Antigens, Viral, Cell Line, Chromatography, High Pressure Liquid, HIV-1, Histocompatibility Antigens Class I, Humans, T-Lymphocytes, Cytotoxic, Tandem Mass Spectrometry