Michael S. Bereman Distinguished Lecture in Analytical Chemistry

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About the Seminar:

Title:

Post-translational Modifications as Clues to Disease and Infection

Abstract:

Determination of the relationship between changes in tissue and circulating forms and levels of proteins and their derivative peptides and the development of disease- or age- related physiological changes poses major challenges because of the broad dynamic range of the biologically active species, the structural complexity and diversity of co- and post-translational modifications, and the presence of numerous isomeric structures in biological samples. We are developing and applying mass spectrometry-centered methods that are compatible with on-line separations (pre- and post-ionization) and electron-based dissociation modes that preserve labile protein modifications while producing highly informative fragmentation. Illustrations will include examples from earlier work that drove the development of current approaches. Recent and ongoing studies utilize a variety of MS techniques that enable comprehensive proteomic and glycoproteomics analyses of clinical samples and model cell systems that are relevant to increased understanding of the pathways underlying protein misfolding disorders, tools for combating cancer and infectious diseases, and development of vaccines.

About the Speaker:

Catherine E. Costello is a Professor in the Dept. of Biochemistry, Cell Biology, and Genomics and holds secondary appointments in Physiology and Biophysics at BUSM and Chemistry on the CRC. She earned her AB at Emmanuel College, Boston, and Ph.D. at Georgetown Univ., Washington, DC, and was a postdoctoral fellow and Senior Research Scientist at MIT. She founded the BU School of Medicine Center for Biomedical Mass Spectrometry in 1994. Her research centers on development and application of MS-based methods to study glycobiology, protein post-translational modifications, folding disorders, cardiovascular and infectious diseases, and bioactive lipids. Major current development projects include Mass Spectrometry Imaging using Matrix-Assisted laser Desorption/Ionization, with emphasis on its application to Chronic Traumatic Encephalopathy (CTE) and Traumatic Brain Injury (TBI); Ion Mobility Coupled to Mass Spectrometry, particularly for the characterization of glycans, glycoconjugates, and protein complexes; and exploration of the fragmentation pathways for glycans and glycoconjugates initiated by Electron-based Dissociation methods (ExD). Current collaborative studies include glycan mapping and structural determinations in cancer, signaling, infectious diseases and archaea, protein post-translational modifications that are evidence of oxidative stress, investigations of HLA-DR antigen presentation in Lyme Disease and Rheumatoid Arthritis, MS-based studies of CTE and TBI, the adaptation of ExD to Ion Mobility MS, applications of Ion Mobility and cross-linking to understanding protein misfolding in systemic amyloid and prion diseases, and RNA binding proteins of Trypanosomes.

She has authored ~350 scientific papers. She is President of the International Mass Spectrometry Foundation, a member of the Boards of Directors of US-HUPO and the Malta Conferences Foundation, a Councilor of the American Chemical Society,  and a member of several editorial and advisory boards. She served as President of the American Society for Mass Spectrometry (2002-04) and President of the Human Proteome Organization (2011-12). She has received the HUPO Awards for Discovery in Proteomics and Contributions to Proteomics, the IMSF Thomson Medal, and the ACS Field and Franklin Award, and is an ACS Fellow.