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  • PMID: 26483422 was deleted because it is a duplicate of PMID: 26628741
Mol Cell Proteomics. 2015 Dec;14(12):3105-17. doi: 10.1074/mcp.M115.052431.

Analysis of Major Histocompatibility Complex (MHC) Immunopeptidomes Using Mass Spectrometry.

Author information

1
From the ‡Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; caron@imsb.biol.ethz.ch aebersold@imsb.biol.ethz.ch.
2
§Department of Immunology, Interfaculty Institute for Cell Biology, University of Tübingen, Tübingen, Germany;
3
From the ‡Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland;
4
From the ‡Department of Biology, Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland; ¶Faculty of Science, University of Zurich, Zurich, Switzerland caron@imsb.biol.ethz.ch aebersold@imsb.biol.ethz.ch.

Abstract

The myriad of peptides presented at the cell surface by class I and class II major histocompatibility complex (MHC) molecules are referred to as the immunopeptidome and are of great importance for basic and translational science. For basic science, the immunopeptidome is a critical component for understanding the immune system; for translational science, exact knowledge of the immunopeptidome can directly fuel and guide the development of next-generation vaccines and immunotherapies against autoimmunity, infectious diseases, and cancers. In this mini-review, we summarize established isolation techniques as well as emerging mass spectrometry-based platforms (i.e. SWATH-MS) to identify and quantify MHC-associated peptides. We also highlight selected biological applications and discuss important current technical limitations that need to be solved to accelerate the development of this field.

PMID:
26628741
PMCID:
PMC4762616
DOI:
10.1074/mcp.O115.052431
[Indexed for MEDLINE]

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