Catherine Fenselau (Presenter)
University of Maryland
Bio: Catherine Fenselau received an A.B. from Bryn Mawr College and her Ph.D. at Stanford University, where she joined Carl Djerassi in the first studies of mass spectrometric fragmentation of amines, amides and esters. As one of the first trained mass spectrometrists to be appointed to the faculty of a U.S. medical school (Johns Hopkins), she has been a leader for several decades in biomedical applications of mass spectrometry. At Hopkins her group was the first to elucidate the structure of the active metabolite of the widely used anticancer agent cyclophosphamide (Cancer Research 1973). With collaborators from the FDA she discovered that the structure of the controversial antitumor compound being sold as Laetrile was a glycoside, not the patented glucuronide (Science 1977). With John Anhalt she first demonstrated that bacteria could be distinguished at the species level by direct desorption of intact chemical biomarkers into the mass spectrometer (Anal. Chem. 1975). Her team continued this research for several decades, notably demonstrating that proteomic strategies can be used to identify bacteria, yeast and some viruses without library matching (Anal. Chem. 1975). Work in her laboratory and others laid the groundwork for the recent approval by the FDA of MALDI-TOF for clinical microbiology and for its current use in hospitals worldwide. In 1988 she moved her laboratory to UMBC, where among many contributions, her team used a four sector tandem mass spectrometer to make the first experimental determination of the proton affinity of arginine (Rapid Commun. Mass Spectrom. 1992). She is presently Professor of Chemistry & Biochemistry at the University of Maryland College Park, with secondary appointments in the Greenebaum Cancer Center and the Bioengineering Department. Current funded research addresses the role of proteins in suppression of the tumor immune response by myeloid-derived suppressor cells (J. Proteome Res. 2014); proteins and their functions in exosomes (J. Proteome Res. 2016); the analysis of polyubiquitins (branched proteins) using top-down proteomics (J. Mass Spectrometry 2016); and continued studies of proteins as forensic biomarkers.
Authorship: Catherine Fenselau
University of Maryland, College Park MD, USA
| Short Abstract Various configurations of MALDI mass spectrometry have been developed for rapid detection of unprocessed microorganisms on the battle field. Recently this direct approach has been approved by the FDA for use in clinical microbiology. Automated data processing has a critical role in both of these applications, and both library matching and proteomic bioinformatics have been developed to identify bacteria based on their mass spectra. This presentation will include a historical overview of the biomarkers, including phospholipids and proteins, which can be observed directly from unprocessed bacteria and yeast using many different ionization methods. Observations will be offered on strategies for sample enrichment. Current limitations and challenges for mass spectrometry-based strategies will be discussed. |
Long Abstract
Various configurations of MALDI mass spectrometry have been developed for rapid detection of unprocessed microorganisms on the battle field. Recently this direct approach has been approved by the FDA and the EU for use in clinical microbiology and is established in several thousand hospitals around the globe. Automated data processing has a critical role in both of these applications, and both library matching and proteomic bioinformatics have been developed to identify bacteria based on their mass spectra. This presentation will include a historical overview of the biomarkers, including metabolites, phospholipids and proteins, which can be observed directly from unprocessed bacteria and yeast using electron impact, fast atom bombardment, MALDI, electrospray and other ambient ionization methods. Observations will be offered on strategies for sample enrichment. The pros and cons will be presented for the use of proteomic bioinformatics, for example, accommodation of different sample preparations and different ionization techniques. Sensitivity, reproducibility, phenotypic resolution and other requirements will be discussed, as well as current limitations and challenges for such mass spectrometric strategies.
References & Acknowledgements:
| Description | Y/N | Source |
| Grants | yes | ZeteoTech |
| Salary | no | |
| Board Member | no | |
| Stock | no | |
| Expenses | no |
IP Royalty: no
| Planning to mention or discuss specific products or technology of the company(ies) listed above: | no |