MHC class I molecules present short peptides derived from intracellular proteins at the cell surface, which enables CD8+ T cells to 'screen' these cells for signs of infection or cancer. Defining the exact peptide repertoire of MHC class I molecules could aid the design of vaccines and other immunotherapies. A new study describes an improved mass spectrometry-based method for identifying such peptides. Mommen et al. found that combined electron-transfer and higher-energy collision dissociation increased the detectable peptide repertoire by approximately threefold compared with more established techniques. This study offers some interesting new insights: in particular, although previous work suggested that each intracellular protein is represented by only a single peptide on MHC class I molecules, the authors' data indicate that at least two peptides from most proteins are presented at the cell surface.
References
Mommen, G. P. M. et al. Expanding the detectable HLA peptide repertoire using electron-transfer/higher-energy collision dissociation (EThcD). Proc. Natl Acad. Sci. USA http://dx.doi.org/10.1073/pnas.1321458111 (2014)
Rights and permissions
About this article
Cite this article
Bordon, Y. Expanding the detectable peptide repertoire. Nat Rev Immunol 14, 214 (2014). https://doi.org/10.1038/nri3659
Published:
Issue Date:
DOI: https://doi.org/10.1038/nri3659