This proposal requests $600,000 towards the purchase of an orbitrap fusion tribrid HPLC- mass spectrometer to be put to work in the Proteomics Facility at the University of Maryland. A consortium of interest centers across the campus will provide the $262,077 match required to meet the full price of the system. Four major and eight minor users describe research projects that will benefit significantly from access to the sensitivity, cycle time and efficient ion activation of the state-of-the-art system. An experienced Facility Director and responsible management and financial plans are described. Ninety per cent of the instrument time is allocated to NIH-supported research. Many of the projects address critical changes that occur in proteins in both pathogens and host organisms during and resulting from infection. The new mass spectrometer will also advance understanding of the mechanisms by which ubiquitin conjugation controls the fate of many proteins in healthy and diseased cells.

Agency
National Institute of Health (NIH)
Institute
Office of The Director, National Institutes of Health (OD)
Type
Biomedical Research Support Shared Instrumentation Grants (S10)
Project #
1S10OD019938-01
Application #
8823243
Study Section
Special Emphasis Panel (ZRG1-BCMB-A (30))
Program Officer
Levy, Abraham
Project Start
2015-03-15
Project End
2016-03-14
Budget Start
2015-03-15
Budget End
2016-03-14
Support Year
1
Fiscal Year
2015
Total Cost
$600,000
Indirect Cost
Name
University of Maryland College Park
Department
Chemistry
Type
Schools of Earth Sciences/Natur
DUNS #
790934285
City
College Park
State
MD
Country
United States
Zip Code
20742
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Chen, Dapeng; Gomes, Fabio; Abeykoon, Dulith et al. (2018) Top-Down Analysis of Branched Proteins Using Mass Spectrometry. Anal Chem 90:4032-4038
Geis-Asteggiante, Lucía; Belew, Ashton T; Clements, Virginia K et al. (2018) Differential Content of Proteins, mRNAs, and miRNAs Suggests that MDSC and Their Exosomes May Mediate Distinct Immune Suppressive Functions. J Proteome Res 17:486-498
Chauhan, Sitara; Danielson, Steven; Clements, Virginia et al. (2017) Surface Glycoproteins of Exosomes Shed by Myeloid-Derived Suppressor Cells Contribute to Function. J Proteome Res 16:238-246
Lee, Amanda E; Geis-Asteggiante, Lucia; Dixon, Emma K et al. (2016) Preparing to read the ubiquitin code: top-down analysis of unanchored ubiquitin tetramers. J Mass Spectrom 51:629-637
Lee, Amanda E; Geis-Asteggiante, Lucia; Dixon, Emma K et al. (2016) Preparing to read the ubiquitin code: characterization of ubiquitin trimers by top-down mass spectrometry. J Mass Spectrom 51:315-21
Geis-Asteggiante, Lucía; Ostrand-Rosenberg, Suzanne; Fenselau, Catherine et al. (2016) Evaluation of Spectral Counting for Relative Quantitation of Proteoforms in Top-Down Proteomics. Anal Chem 88:10900-10907