Peptides eluted from HLA-B27 of human splenocytes and blood cells reveal a similar but partially different profile compared to in vitro grown cell lines

• Published in: Immunology letters Vol. 94; no. 3; pp. 261 - 265
• Main Authors: Stodůlková, Eva, Man, Petr, Pohl, Jan, Van Nguyen, Dung, Vaingátová, Silvie, Ivašková, Eva, Pla, Marika, Čapková, Jana, Sedláčková, Marie, Ivanyi, Pavol, Flieger, Miroslav
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 15.07.2004
• Subjects: Cells, Cultured; HLA-B ∗2705; HLA-B27 Antigen - chemistry; HLA-B27 Antigen - immunology; Humans; LC–MS/MS analysis; Lymphocytes - immunology; Peptide Fragments - chemistry; Peptide Fragments - immunology; Peptide profile; Peptide sequence; Spleen - immunology; BC; SpA; HLA-B ∗2705; LC–MS/MS analysis; Peptide sequence; MHC; HLA; Peptide profile
• ISSN: 0165-2478; 1879-0542
• DOI: 10.1016/j.imlet.2004.05.016

The sequences and profiles of peptides which bind to HLA-B ∗2705 splenocytes and peripheral blood cells were compared with those previously published from in vitro long-term cell cultures. B ∗2705 peptide profile analysed by solid-phase Edman degradation and 15 individual peptide sequences determined by LC–MS/MS were partially similar to those defined from in vitro long-term cell cultures. Arg at P2 was found in 11 of 15 sequenced peptides (73.3%). This value is lower in comparison with other published data. Two sequences were matching to unknown proteins, which displayed similarity with myosin. These are first data on peptide sequences isolated directly from HLA-B27 molecules without prior in vitro propagation of the cells.