Ulrich Eckhard
Post-doctoral fellow (2012-2016)
Funded by the MSFHR
Centre for Blood Research
University of British Columbia
2350 Health Sciences Mall
Vancouver, BC, V6T 1Z3, Canada
Lab: #4.420; Bench 5
Phone: +1-604-822-3561 (lab)
Email: ulrich.eckhard@ubc.ca
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Biographical Sketch
During my PhD at the University of Salzburg (2007-2011), I focused on the enzymatic and structural characterization of three bacterial collagenases. I successfully expressed, purified, crystallized and determined the structure of collagenase G and H from C. histolyticum, and collagenase T from C. tetani, allowing us to solve the long-standing and intractable puzzle of clostridial collagenolysis. This structural breakthrough together with my biochemical analysis paved the way for how we now envision the turnover of collagen―the most abundant protein in man and one of the most challenging substrates―by bacterial collagenases.
In 2012 I switched gears and joined the lab of Prof. Chris Overall at the University of British Columbia, Vancouver. Over the last four years, I mastered several cutting-edge omics-based techniques including the positional proteomics technique TAILS (Terminal Amine Isotopic Labeling of Substrates) and the high-throughput protease profiling method PICS (Proteomic Identification of protease Cleavage Sites). I participated in many interdisciplinary and collaborative projects, including profiling various protease families (e.g. type II transmembrane serine proteases, matrix metalloproteinaseses) and elucidating proteolytic processing in health and disease (e.g. dental pulp, skin inflammation).
I have a strong and comprehensive background in protein biochemistry, biophysical methods, and a high level of enthusiasm and team spirit needed for successful research. I love to engage in high quality research, being part of a vibrant team, learning new techniques, and taking up new challenges.
For a full research profile, list of publications and contact details, please visit my ResearchGate or LinkedIn profile, or check out my wordpress page.
Education
- 2007 – 2012: Doctor of Philosophy (PhD), Molecular Biology; University of Salzburg, Austria
- 2006 – 2011: Master of Science (M.Sc.), Molecular Biology; Universities of Salzburg and Linz, Austria
- 2005 – 2007: Master of Science (M.Sc.), Genetics; University of Salzburg, Austria
- 2004 – 2006: Bachelor of Science (B.Sc.), Molecular Bioscience; Universities of Salzburg and Linz, Austria
- 2001 – 2005: Bachelor of Science (B.Sc.), Biology; University of Salzburg, Austria
Publications
- Eckhard U, Marino G, Abbey SR, Tharmarajah G, Matthew I, and Overall CM ( 2015). The Human Dental Pulp Proteome and N-Terminome: Levering the Unexplored Potential of Semitryptic Peptides Enriched by TAILS to Identify Missing Proteins in the Human Proteome Project in Underexplored Tissues. J Proteome Res. 2015 Sep 4;14(9):3568-82. PMID: 26258467.
- Marino G, Eckhard U, and Overall CM. (2015). Protein Termini and Their Modifications Revealed by Positional Proteomics. ACS Chem Biol. 2015 Aug 21;10(8):1754-64. PMID: 25331112.
- Huesgen PF, Lange PF, Rogers LD, Solis N, Eckhard U, Kleifeld O, Goulas T, Gomis-Rüth FX, and Overall CM (2014). LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification. Nat Methods. 2015 Jan;12(1):55-8. PMID: 25419962.
- Prudova A, Serrano K, Eckhard U, Fortelny N, Devine DV, and Overall CM (2014). TAILS N-terminomics of human platelets reveals pervasive metalloproteinase dependent proteolytic processing in storage. Blood. 2014 Dec 18;124(26):e49-60. PMID: 25331112.
- Barré O, Dufour A, Eckhard U, Kappelhoff R, Béliveau F, Leduc R, and Overall CM (2014). Cleavage specificity analysis of six type II transmembrane serine proteases (TTSPs) using PICS with proteome-derived peptide libraries. PLoS One 9(9):e105984, PMID: 25211023.
- Eckhard U, Huesgen PF, Brandstetter H, and Overall CM (2014). Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen. Journal of Proteomics, 100, 102-114. PMID: 24125730.
- Marino G, Huesgen PF, Eckhard U, Overall CM, Schröder WP, and Funk C (2014). Family-wide characterization of Matrix Metallo-proteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity. Biochemical Journal. 457:2, 335-346. PMID: 24156403.
- Eckhard U, Schönauer E, and Brandstetter H (2013). Structural basis for activity regulation and substrate specificity of clostridial collagenases G, H, and T. Journal of Biological Chemistry, 288:28, 20184-20194. PMID: 23703618.
- auf dem Keller U, Prudova A, Eckhard U, Fingleton B, and Overall CM (2013). Systems-level analysis of proteolytic events in increased vascular permeability and complement activation in skin inflammation. Science Signaling, 6:258, rs2.
- Kofler S, Asam C, Eckhard U, Wallner M, Ferreira F, Brandstetter H (2012). Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1. Journal of Molecular Biology, 422:1, 109-123. PMID: 22634284
- Eckhard U, Schönauer E, Nüss D & Brandstetter H (2011). Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis. Nature Structural & Molecular Biology, 18:10, 1109-1114. PMID: 21947205.
- Eckhard U and Brandstetter H (2011). Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment. Biological Chemistry, 392:11, 1039-1045. PMID: 21871007.
- Ducka P, Eckhard U, Schönauer E, Kofler S, Gottschalk G, Brandstetter H and Nüss D (2009). A universal strategy for high-yield production of soluble and functional clostridial collagenases in E. coli. Applied Microbiology and Biotechnology, 83:6. 1055-1065. PMID: 19333597.
- Eckhard U, Schönauer E, Ducka P, Briza P, Nüss D and Brandstetter H (2009). Biochemical characterization of the catalytic domains of three different clostridial collagenases. Biological Chemistry, 390:1, 11-18. PMID: 18937627.
- Eckhard U, Nüss D, Ducka P, Schönauer E and Brandstetter H (2008). Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum. Acta Crystallographica Section F 64:5, 419-421. PMID: 18453715.