The Mass Spectrometry core has been renamed the Mass Spectrometry and Biological Structure (MSBS) Core to reflect increased importance of protein structure analysis. An expert in NMR, Professor Rachel Klevit, has been added to the core as well as an expert in silico protein structure prediction (PSP), Dr Lars Malmstrom. The mass Spectrometry expert remains Professor David Goodlett. As such the core maintains its original goals of providing qualitative and quantitative proteomic analysis, protein post-translational modification analysis, as well as lipid A structure analysis. However, we note that the revised core is devoted to applications of analytical methods as opposed to development of methods in which the original core was engaged. We will use our bioanalytical expertise to conduct the following specific aims on behalf of NWRCE investigators: 1) Determine structures of proteins and protein complexes; 2) Determine structures of small molecules and screen libraries; 3) Characterize Global Protein Regulation;and 4) Consult and Train NWRCE Investigators on Aims 1 - 3. To carry out these aims we will utilize a number of technologies including, but not limited to, the following: 1) High Performance Liquid Chromatography - Electrospray lonization - Tandem Mass Spectrometry. 2) Matrix Assisted Laser Desorption lonization Time-of-Flight Mass Spectrometry. 3) Nuclear Magnetic Resonance Spectroscopy. 4) Computational methods to support interpretation of data.

Public Health Relevance

The Mass Spectrometry and Biological Structure (MSBS) Core provides support for NWRCE investigators to define function of molecules (i.e. proteins and small molecules) through structural analysis and discoverybased profiling experiments. The supported projects primarily seek to discovery new proteins (e.g. therapeutic targets) and lipids (e.g. new vaccine adjuvants) involved in virulence or to define new roles for known molecules.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Specialized Center--Cooperative Agreements (U54)
Project #
5U54AI057141-10
Application #
8447095
Study Section
Special Emphasis Panel (ZAI1-DDS-M)
Project Start
Project End
2015-02-28
Budget Start
2013-03-01
Budget End
2014-02-28
Support Year
10
Fiscal Year
2013
Total Cost
$206,025
Indirect Cost
$64,909
Name
University of Washington
Department
Type
DUNS #
605799469
City
Seattle
State
WA
Country
United States
Zip Code
98195
West, T Eoin; Myers, Nicolle D; Chantratita, Narisara et al. (2014) NLRC4 and TLR5 each contribute to host defense in respiratory melioidosis. PLoS Negl Trop Dis 8:e3178
Hagar, Jon A; Miao, Edward A (2014) Detection of cytosolic bacteria by inflammatory caspases. Curr Opin Microbiol 17:61-6
Majerczyk, Charlotte D; Brittnacher, Mitchell J; Jacobs, Michael A et al. (2014) Cross-species comparison of the Burkholderia pseudomallei, Burkholderia thailandensis, and Burkholderia mallei quorum-sensing regulons. J Bacteriol 196:3862-71
Loomis, Wendy P; Johnson, Matthew L; Brasfield, Alicia et al. (2014) Temporal and anatomical host resistance to chronic Salmonella infection is quantitatively dictated by Nramp1 and influenced by host genetic background. PLoS One 9:e111763
Martínez, Luary C; Vadyvaloo, Viveka (2014) Mechanisms of post-transcriptional gene regulation in bacterial biofilms. Front Cell Infect Microbiol 4:38
Myers, Nicolle D; Chantratita, Narisara; Berrington, William R et al. (2014) The role of NOD2 in murine and human melioidosis. J Immunol 192:300-7
Correia, Bruno E; Bates, John T; Loomis, Rebecca J et al. (2014) Proof of principle for epitope-focused vaccine design. Nature 507:201-6
Majerczyk, Charlotte; Brittnacher, Mitchell; Jacobs, Michael et al. (2014) Global analysis of the Burkholderia thailandensis quorum sensing-controlled regulon. J Bacteriol 196:1412-24
Pruneda, Jonathan N; Smith, F Donelson; Daurie, Angela et al. (2014) E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis. EMBO J 33:437-49
Sureka, Kamakshi; Choi, Philip H; Precit, Mimi et al. (2014) The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function. Cell 158:1389-401

Showing the most recent 10 out of 184 publications