Donald Frederick Hunt

Pioneered efforts to develop methods and instrumentation that set the standard for ultrasensitive detection and characterization of proteins and peptides.  These contributions continue to underpin the whole field of proteomics and have had a dramatic impact on research in immunology, cell signaling, cell migration, epigenetics and cancer.   Was first to employ tandem mass spectrometry to characterize peptides presented to the immune system by class I and Class II MHC molecules.     Peptides recognized by cytotoxic T-lymphocytes specific for tumors, graft vs host disease, viral and bacterial epitopes, and type 1 diabetes have all been discovered by the Hunt group. Showed that class I MHC phosphopeptides differentially expressed on cancer cells are likely candidates for adoptive T-cell therapy and vaccines against cancer. The Hunt lab also pioneered methods for the enrichment and characterization of protein post-translational modifications such as phosphorylation. GlcNAcylation and the multiple marks that constitute the “histone code”.   Recent achievements include development of instrumentation that makes it possible to use ion-ion chemistry inside the mass spectrometer to determine the sequence of amino acids at both the n-terminus and c-terminus of intact proteins and to completely sequence large protein fragments.  This technique, electron transfer dissociation (ETD), facilitates identification of proteins in complex mixtures on a chromatographic time-scale, and allows one to detect the presence of both splice variants and post-translational modifications.