作者: Hugo D. Meiring , Betsy Kuipers , Jacqueline A. M. van Gaans-van den Brink , Martien C. M. Poelen , Hans Timmermans
DOI: 10.4049/JIMMUNOL.174.9.5636
关键词:
摘要: The meningococcal class I outer membrane protein porin A plays an important role in the development of T cell-dependent protective immunity against serogroup B infection and is therefore a major component candidate vaccines. cell epitopes from are poorly characterized because weak vitro memory responses purified Ag strain variation. We applied novel strategy to identify relevant naturally processed MHC II-presented epitopes, based on stable isotope labeling Ag. Human immature HLA-DR1-positive dendritic cells were used for optimal uptake II processing (14)N- (15)N-labeled isoforms neisserial serosubtype P1.5-2,10 bacterial vesicles. HLA-DR1 bound peptides, obtained after 48 h processing, contained typical spectral doublets mass spectrometry that could easily be assigned four regions, expressed at diverging densities ( approximately 30-4000 copies/per cell). Epitopes two these regions recognized by HLA-DR1-restricted CD4(+) lines conserved among different serosubtypes A. This tag-assisted approach provides useful methodology rapid identification presented vaccine development.