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Mass Tag-Assisted Identification of Naturally Processed HLA Class II-Presented Meningococcal Peptides Recognized by CD4⁺ T Lymphocytes

Hugo D. Meiring^*, Betsy Kuipers, Jacqueline A. M. van Gaans-van den Brink, Martien C. M. Poelen, Hans Timmermans, Gino Baart, Humphrey Brugghe, Joost van Schie, Claire J. P. Boog, Ad P. J. M. de Jong^* and Cécile A. C. M. van Els^1,

^* Laboratory of Analytical Chemistry, National Institute of Public Health and the Environment, Laboratories of Vaccine Research and Product and Process Development, Netherlands Vaccine Institute, Bilthoven, The Netherlands

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

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