Associate Professor
Dr. Paul Hensbergen
RESEARCH
The research of Paul Hensbergen primarily focuses on microbial proteomics, e.g. structure and function of bacterial proteases, Clostridioides difficile (C diff) phosphoproteomics, biosynthesis of a glycan modification on C diff flagellin C, antibiotic resistance in Gram-negative bacteria and MS-methods to type bacteria. This research is based on a long-standing, close collaboration with the Experimental Bacteriology group of the LUMC (dr. J Corver and dr. Wiep Klaas Smits). His main interest is a novel class of bacterial metalloproteases that cleave between two prolines (for which they coined the name Pro-Pro endopeptidase (PPEP)). The LUMC team identified the first member (PPEP-1 in Clostridioides difficile) in 2014, followed by the second member in Paenibacillus alvei (PPEP-2) in 2018. Currently, he coordinates a PPEP-project that was funded by the Dutch Research Council (NWO) in 2020. In addition to his microbial proteomics work, he is involved in several research projects in which the CPM Proteomics group participates, primarily related to (cancer) glycoproteomics. He also coordinates the teaching activities of the CPM.
CURRICULUM VITAE
Paul Hensbergen studied Biology at the Vrije University (VU) in Amsterdam and obtained his PhD in ecotoxicology (Thesis title: Metallothionein in Orchesella cincta) at the same university in 1999. After a post-doc at the Dept. of Dermatology (cancer proteomics and chemokine receptor signaling), first at the VU, later at the LUMC, he moved to the biomolecular mass spectrometry group of the Dept. of Parasitology that later became part of the current Center for Proteomics and Metabolomics (CPM). At the CPM, he is part of the proteomics subgroup. In addition to his research activities, he is co-coordinator of the Frontiers of Science course “Proteomics in Biomedical Research” as part of the Master Biomedical Sciences. Moreover, he is a member of several teaching committees of this Master program.
Publications
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A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins
Hensbergen PJ, Klychnikov OI, Bakker D, van Winden VJ, Ras N, Kemp AC, Cordfunke RA, Dragan I, Deelder AM, Kuijper EJ, Corver J, Drijfhout JW, van Leeuwen HC
Mol. Cell Proteomics (2014), 13:1231-1244. doi: 10.1074/mcp.M113.034728
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Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831
Hensbergen PJ, Klychnikov OI, Bakker D, Dragan I, Kelly ML, Minton NP, Corver J, Kuijper EJ, Drijfhout JW, van Leeuwen HC.
FEBS Lett (2015), 589: 3952-3958. doi: 10.1016/j.febslet.2015.10.027
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Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family
Klychnikov OI, Shamorkina TM, Weeks SD, van Leeuwen HC, Corver J, Drijfhout JW, van Veelen PA, Sluchanko NN, Strelkov SV, Hensbergen PJ
J. Biol. Chem. (2018). 293: 11154-11165. doi: 10.1074/jbc.RA118.003244
Groups:
Proteomics | Team
