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David Colquhoun received his B.Sc. (Hons) from the University of Sunderland, where he studied Applied and Industrial Microbiology. He earned a M.S. in Microbiology at Michigan Technological University, and received a Ph.D. at Johns Hopkins Bloomberg School of Public Health under Dr. Rolf Halden. His work focused on the application of quantitative protein biomarkers to public health research. This work utilized most of the techniques for quantitative gel- and mass spectrometry (MS)-based proteomics. Dr. Colquhoun was hired in the Johns Hopkins School of Medicine Mass Spectrometry and Proteomics Facility, where he assisted with high thoughput protein MS and gel electrophoresis, and worked on post-translational modification and measurement of intact proteins. Dr. Colquhoun was recruited to the Retrovirus laboratory by Dr. Graham as a proteomics specialist, and subsequently joined the faculty in 2011.
Dr. Colquhoun’s research in the Graham Lab is focused on identifying and characterizing host and viral proteins, their modifications (PTMs) and interactions. This is achieved using a combination of native, one- and two- dimensional gel electrophoresis, offline- and online- liquid chromatography separations and mass spectrometry. We have coupled these techniques with Click chemistry labeling of PTMs to visualize, enrich and quantify the host responses to infection, and identify novel HIV-interacting pathways and proteins, in particular those related to lipid rich microdomains in the membrane, where viruses are known to interact. Dr. Colquhoun’s current work is studying the acylproteome, enriching and identifying proteins containing lipid modifications. He has utilized high resolution MS, confocal microscopy and two dimensional gel electrophoresis to measure the location and identity of modified proteins. Using MS and bioinformatic data analysis, he is identifying host pathways whose modifications are altered during HIV infection.
Dr. Colquhoun is a member of the JHU NHLBI Proteomics Initiative and the Programs of Excellence in Glycosciences (PEG). Both of these programs support development of novel MS techniques and biomarker discoveries. Within these programs, the Graham Lab is studying cardiac disease in the context of proteins (NHLBI) and glycan modifications (PEG). In this, we are working on developing novel MS analysis techniques, such as glycan MS, metabolomics, and MS tissue imaging. Our goal is to integrate these many data inputs in all of our experiments in order to develop true system biology models for data analysis and discovery efforts.
· Travel Honorarium, ASMS Fall Workshop, San Diego, CA
· Kazuyoshi Kawata Fund in Sanitary Science and Engineering Award
· American Society for Microbiology Corporate Activities Program Travel Grant
· Cornelius Krusé Award for Outstanding Thesis in Environmental Health, JHSPH
Colquhoun, D. R., L. R. Goldman, R. N. Cole, M. Gucek, M. Mansharamani, F. R. Witter, B. J. Apelberg, and R. U. Halden. 2009. Global Screening of Human Cord Blood Proteomes for Biomarkers of Toxic Exposure and Effect. Environ Health Perspect 117:832–838.
Hartmann, E.M., D. R. Colquhoun, R. U. Halden. 2010. Identification of Putative Biomarkers for Toluene-Degrading Burkholderia and Pseudomonads by Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry and Peptide Mass Fingerprinting. Biosci. Biotechnol. Biochem. 74(7):1470 – 1472.
Parish, L.A., D. R. Colquhoun, C. Ubaida-Mohien, A. Lyashkov, D. R. Graham, R. R. Dinglasan. 2011. Ookinete-Interacting Proteins on the Microvillar Surface are Partitioned into Detergent Resistant Membranes of Anopheles gambiae Midguts. J Proteome Res. 10 (11):5150-62.