Abstract:
:As a tetrameric major histocompatibility complex (MHC) class I-peptide complex (tetramer) is capable of detecting antigen-specific cytotoxic T lymphocyte (CTL) by flow cytometry, significant information about the generation of in vivo immunity can be obtained. It is, however, difficult to make a soluble wild type of MHC class I heavy chain by the prokaryotic expression system. Therefore, we developed a new method for making soluble mutant HLA-A*2402 heavy chain. In this method, signal sequences were deleted, and the codon was changed to silent mutated nucleotide sequences that bacteria could use as preferable codon. When purified mutant HLA-A*2402 molecules were examined for the protein generation by SDS-polyacrylamide gel electrophoresis (PAGE) and western blotting using anti-HLA class I monoclonal antibody (mAb) as compared with wild type, a large amount of mutant heavy chain could be detected. In contrast, the expression of wild-type stable HLA-A*2402 heavy chain molecule was not detected in this system. Consequently, by using mutant HLA-A*2402/peptide tetramers, CTL precursors (CTLp) that specifically recognize antigenic peptide derived from the X;18 chromosomal translocations of synovial sarcoma were detected in patients' PBL.
journal_name
J Immunol Methodsjournal_title
Journal of immunological methodsauthors
Sato Y,Sahara H,Tsukahara T,Kondo M,Hirohashi Y,Nabeta Y,Kawaguchi S,Ikeda H,Torigoe T,Ichimiya S,Tamura Y,Wada T,Yamashita T,Goto M,Takasu H,Sato Ndoi
10.1016/s0022-1759(02)00329-0keywords:
subject
Has Abstractpub_date
2002-12-20 00:00:00pages
177-84issue
1-2eissn
0022-1759issn
1872-7905pii
S0022175902003290journal_volume
271pub_type
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