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NL

dr. T. (Tanneke) den Blaauwen

Faculty of Science
Swammerdam Institute for Life Sciences

Visiting address
  • Science Park 904
  • Room number: C3.108
Postal address
  • Postbus 94232
    1090 GE Amsterdam
  • Molecular mechanism of bacterial morphogenesis and antibiotic target validation

    Research

    The morphology of rod shaped bacteria is achieved through two very dynamic synthetic complexes: the elongasome and the divisome. The elongasomes are recruited by the actin-like cytoskeleton MreB protein underneath the plasma membrane and move in an helical path to insert new peptidoglycan subunits to elongate the cell envelope whereas the divisome is responsible for division and the synthesis of new cell poles. Cell division is directed by the FtsZ ring (a tubulin homolog) that directs the synthesis of the new cell poles  during binary fission by treadmilling in a ring underneath the cytoplasmic membrane. The assembly and the dynamics of the elongasome and divisome are studied in vivo using immunofluorescence and fluorescence microscopy techniques (FRET, FLIM, FRAP, immunolocalization) and in vitro using state of the art biochemical and biophysical techniques. By aiming to obtain quantitative data on number of proteins, their affinities for each other or their substrates and their localization as function of the bacterial division cycle, we hope to model the measured and observed interactions. Similar studies are directed to the insertion of outer membrane proteins and the lipid and LPS transport systems that enable envelope membrane growth. The crosstalk between these protein machines could provide new targets for antibiotics that attack multiple essential pathways in the cell and so make it much harder for the bacteria to become resistant to these antibiotics.

    Figure 1. A. Schematic presentation of the timing of cell division cycle event. B. Many proteins are involved in cell division and are collectively termed the divisome. About 50 synthetic complexes (green spheres) are recruited by the FtsZ ring (orange ring). While the ring constrict the synthetic complexes synthesize the new cell poles and split the  envelope between the two daughter cells simultaneously. C. MreB polymers underneath the cytoplasmic membrane recruit the synthetic complexes  (elongasomes) involved in length growth.

  • CV

    CV

    • 2012 Associate professor at the University of Amsterdam, Faculty of Sciences, Swammerdam Institute for Life Sciences, section Bacterial cell Biology.
    • 2011 Associate professor at the University of Amsterdam, Faculty of Sciences, Swammerdam Institute for Life Sciences, section Molecular Cytology.
    • 2006-2011 Assistant professor at the University of Amsterdam, Faculty of Sciences, Swammerdam Institute for Life Sciences, section Molecular Cytology.
    • 2001-2006 Postdoc (NWO grant VIDI) at the University of Amsterdam, Faculty of Sciences, Swammerdam Institute for Life Sciences, section Molecular Cytology.
    • 2000-2002 Program coordinator at the University of Amsterdam, Faculty of Sciences, Swammerdam Institute for Life Sciences.
    • 1997-2000 Postdoc at the Molecular Cytology group at the Biology Department of the University of Amsterdam (Grant provided by the forth framework program of the European Community).
    • 1993-1997 Postdoc at the Biology Department of the University of Groningen at the Molecular Microbiology group and associated with the GBB (Groningen Biotechnology and Bioengineering) school of Sciences, (grant provided by NWO pioneer project "protein translocation").
    • 1992-1993 Postdoc at the Mol. Cytol. group at the Biology Department of the University of Amsterdam (Grant provided by the University of Amsterdam).
    • 1991 Work visit at the Oregon Graduate Institute for Science and Technology, Beaverton, Oregon, USA
    • 1989-1992 Postdoc at the Chemistry Department of the Leiden University (grant provided by the Department of Economic affairs/STW).
    • 1985-1988 Ph.D at the Biology Department of the University of, Amsterdam (grant provided by NWO/BION).
  • Publications

    2019

    2018

    2017

    2016

    2015

    • Glas, M., van den Berg van Saparoea, H. B., McLaughlin, S. H., Roseboom, W., Liu, F., Koningstein, G. M., ... Luirink, J. (2015). The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL form a Trimeric Complex with Sub-micromolar Affinity. The Journal of Biological Chemistry, 290(35), 21498-21509. https://doi.org/10.1074/jbc.M115.654756 [details]
    • Gray, A. N., Egan, A. J. F., van 't Veer, I. L., Verheul, J., Colavin, A., Koumoutsi, A., ... Vollmer, W. (2015). Coordination of peptidoglycan synthesis and outer membrane constriction during Escherichia coli cell division. eLife, 4, e07118. https://doi.org/10.7554/eLife.07118 [details]
    • Vischer, N. O. E., Verheul, J., Postma, M., van den Berg van Saparoea, B., Galli, E., Natale, P., ... den Blaauwen, T. (2015). Cell age dependent concentration of Escherichia coli divisome proteins analyzed with ImageJ and ObjectJ. Frontiers in Microbiology, 6, [586]. https://doi.org/10.3389/fmicb.2015.00586 [details]
    • van der Ploeg, R., Goudelis, S. T., & den Blaauwen, T. (2015). Validation of FRET Assay for the Screening of Growth Inhibitors of Escherichia coli Reveals Elongasome Assembly Dynamics. International Journal of Molecular Sciences, 16(8), 17637-17654. https://doi.org/10.3390/ijms160817637 [details]

    2014

    2013

    • Buddelmeijer, N., Aarsman, M., & den Blaauwen, T. (2013). Immunolabeling of Proteins in Situ in Escherichia coli K12 Strains. BIO-PROTOCOL, 3(15). [details]
    • Verhoeven, G. S., Dogterom, M., & den Blaauwen, T. (2013). Absence of long-range diffusion of OmpA in E. coli is not caused by its peptidoglycan binding domain. BMC Microbiology, 13, 66. https://doi.org/10.1186/1471-2180-13-66 [details]
    • den Blaauwen, T. (2013). Prokaryotic cell division: flexible and diverse. Current opinion in microbiology, 16(6), 738-744. https://doi.org/10.1016/j.mib.2013.09.002 [details]
    • van den Berg van Saparoea, H. B., Glas, M., Vernooij, I. G. W. H., Bitter, W., den Blaauwen, T., & Luirink, J. (2013). Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and Fts on the FtsQ protein. The Journal of Biological Chemistry, 288(34), 24340-24350. https://doi.org/10.1074/jbc.M113.485888 [details]
    • van der Ploeg, R., Verheul, J., Vischer, N. O. E., Alexeeva, S., Hoogendoorn, E., Postma, M., ... den Blaauwen, T. (2013). Colocalization and interaction between elongasome and divisome during a preparative cell division phase in Escherichia coli. Molecular Microbiology, 87(5), 1074-1087. https://doi.org/10.1111/mmi.12150 [details]

    2012

    • Banzhaf, M., van den Berg van Saparoea, B., Terrak, M., Fraipont, C., Egan, A., Philippe, J., ... Vollmer, W. (2012). Cooperativity of peptidoglycan synthases active in bacterial cell elongation. Molecular Microbiology, 85(1), 179-194. https://doi.org/10.1111/j.1365-2958.2012.08103.x [details]
    • Leisch, N., Verheul, J., Heindl, N. R., Gruber-Vodicka, H. R., Pende, N., den Blaauwen, T., & Bulgheresi, S. (2012). Growth in width and FtsZ ring longitudinal positioning in a gammaproteobacterial symbiont. Current Biology, 22(19), R831-R832. https://doi.org/10.1016/j.cub.2012.08.033 [details]

    2011

    • Fraipont, C., Alexeeva, S., Wolf, B., van der Ploeg, R., Schloesser, M., den Blaauwen, T., & Nguyen-Distèche, M. (2011). The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli. Microbiology - SGM, 157(1), 251-259. https://doi.org/10.1099/mic.0.040071-0 [details]
    • Kleinschmidt, J. H., Bulieris, P. V., Qu, J., Dogterom, M., & den Blaauwen, T. (2011). Association of neighboring β-strands of outer membrane protein A in lipid bilayers revealed by site-directed fluorescence quenching. Journal of Molecular Biology, 407(2), 316-332. https://doi.org/10.1016/j.jmb.2011.01.021 [details]
    • Olrichs, N. K., Aarsman, M. E. G., Verheul, J., Arnusch, C. J., Martin, N. I., Hervé, M., ... den Blaauwen, T. (2011). A novel in vivo cell-wall labeling approach sheds new light on peptidoglycan synthesis in Escherichia coli. ChemBioChem, 12(7), 1124-1133. https://doi.org/10.1002/cbic.201000552 [details]

    2010

    • Alexeeva, S., Gadella (jr.), T. W. J., Verheul, J., Verhoeven, G. S., & den Blaauwen, T. (2010). Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Molecular Microbiology, 77(2), 384-398. https://doi.org/10.1111/j.1365-2958.2010.07211.x [details]
    • Potluri, L., Karczmarek, A., Verheul, J., Piette, A., Wilkin, J. M., Werth, N., ... den Blaauwen, T. (2010). Septal and lateral wall localization of PBP5, the major D,D-carboxypeptidase of Escherichia coli, requires substrate recognition and membrane attachment. Molecular Microbiology, 77(2), 300-323. https://doi.org/10.1111/j.1365-2958.2010.07205.x [details]
    • Schaffner-Barbero, C., Gil-Redondo, R., Ruiz-Avila, L. B., Huecas, S., Läppchen, T., den Blaauwen, T., ... Andreu, J. M. (2010). Insights into nucleotide recognition by cell division protein FtsZ from a mant-GTP competition assay and molecular dynamics. Biochemistry, 49(49), 10458-10472. https://doi.org/10.1021/bi101577p [details]
    • Soprova, Z., Sauri, A., van Ulsen, P., Tame, J. R. H., den Blaauwen, T., Jong, W. S. P., & Luirink, J. (2010). A conserved aromatic residue in the autochaperone domain of the autotransporter Hbp is critical for initiation of outer membrane translocation. The Journal of Biological Chemistry, 285(49), 38224-38233. https://doi.org/10.1074/jbc.M110.180505 [details]
    • Typas, A., Banzhaf, M., van den Berg van Saparoea, B., Verheul, J., Biboy, J., Nichols, R. J., ... Vollmer, W. (2010). Regulation of peptidoglycan synthesis by outer-membrane proteins. Cell, 143(7), 1097-1109. https://doi.org/10.1016/j.cell.2010.11.038 [details]

    2009

    • Kedrov, A., den Blaauwen, T., & Driessen, A. J. M. (2009). Thermodynamics of the protein translocation. In M. L. Johnson, G. K. Ackers, & J. M. Holt (Eds.), Biothermodynamics, part B (pp. 273-291). (Methods in enzymology; No. 466). Amsterdam: Academic Press. https://doi.org/10.1016/S0076-6879(09)66012-2 [details]
    • Mohammadi, T., Ploeger, G. E. J., Verheul, J., Comvalius, A. D., Martos, A., Alfonso, C., ... den Blaauwen, T. (2009). The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro. Biochemistry, 48(46), 11056-11066. https://doi.org/10.1021/bi901461p [details]
    • Verhoeven, G. S., Alexeeva, S., Dogterom, M., & den Blaauwen, T. (2009). Differential bacterial surface display of peptides by the transmembrane domain of OmpA. PLoS ONE, 4(8), e6739. https://doi.org/10.1371/journal.pone.0006739 [details]

    2008

    2007

    • Jong, W. S., ten Hagen-Jongman, C. M., den Blaauwen, T., Slotboom, J. D., Tame, J. R. H., Wickström, D., ... Luirink, J. (2007). Limited tolerance towards folded elements during secretion of the autotransporter Hbp. Molecular Microbiology, 63(5), 1524-1536. https://doi.org/10.1111/j.1365-2958.2007.05605.x [details]
    • Karczmarek, A., Martinez-Arteaga Baselga, R., Alexeeva, S. V., Hansen, F. G., Vicente, M., Nanninga, N., & den Blaauwen, T. (2007). DNA and origin region segregation are not affected by the transition from rod to sphere after inhibition of Escherichia coli MreB by A22. Molecular Microbiology, 65(1), 51-63. https://doi.org/10.1111/j.1365-2958.2007.05777.x [details]
    • Mohammadi, T., Karczmarek, A., Crouvoisier, M., Bouhss, A., Mengin-Lecreulx, D., & den Blaauwen, T. (2007). The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli. Molecular Microbiology, 65(4), 1106-1121. https://doi.org/10.1111/j.1365-2958.2007.05851.x [details]
    • Norris, V., den Blaauwen, T., Cabin-Flaman, A., Doi, R. H., Harshey, R. M., Janniere, L., ... Skarstad, K. (2007). Functional taxonomy of bacterial hyperstructures. Microbiology and Molecular Biology Reviews, 71(1), 230-253. https://doi.org/10.1128/MMBR.00035-06 [details]
    • Norris, V., den Blaauwen, T., Doi, R. H., Harshey, R. M., Janniere, L., Jimenez-Sanchez, A., ... Thellier, M. (2007). Toward a hyperstructure taxonomy. Annual Review of Microbiology, 61, 309-329. https://doi.org/10.1146/annurev.micro.61.081606.103348 [details]
    • Scheffers, D-J., Robichon, C., Haan, G. J., den Blaauwen, T., Koningstein, G., van Bloois, E., ... Luirink, J. (2007). Contribution of the FtsQ transmembrane segment to localization to the cell division site. Journal of Bacteriology, 189(20), 7273-7280. https://doi.org/10.1128/JB.00723-07 [details]

    2006

    2005

    • Aarsman, M. E. G., Piette, A., Fraipont, C., Vinkenvleugel, T. M. F., Nguyen-Distèche, M., & den Blaauwen, T. (2005). Maturation of the Escherichia coli divisome occurs in two steps. Molecular Microbiology, 55, 1631-1645. https://doi.org/10.1111/j.1365-2958.2005.04502.x [details]
    • Läppchen, T., Hartog, A. F., Pinas, V., Koomen, G. J., & den Blaauwen, T. (2005). GTP analogue inhibits polymerization and GTPase activity of the bacterial protein FtsZ without affecting its eukaryotic homologue tubulin. Biochemistry, 44, 7879-7884. https://doi.org/10.1021/bi047297o [details]
    • Natale, P., den Blaauwen, T., van der Does, C., & Driessen, A. J. M. (2005). Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy. Biochemistry, 44, 6424-6432. https://doi.org/10.1021/bi047488r [details]

    2004

    • Koppelman, C. M., Aarsman, M. E. G., Postmus, J., Pas, E., Muijsers, A. O., Scheffers, D-J., ... den Blaauwen, T. (2004). R174 of Escherichia coli is involved in membrane-interaction and protofilament bundling, and is essential for cell division. Molecular Microbiology, 51, 645-657. https://doi.org/10.1046/j.1365-2958.2003.03876.x [details]
    • Pastoret, S., Fraipont, C., den Blaauwen, T., Wolf, B., Thomas, A., Brasseur, R., ... Nguyen-Distèche, M. (2004). Functional analysis of the cell division protein FtsW of Escherichia coli. Journal of Bacteriology, 186, 8370-8379. https://doi.org/10.1128/JB.186.24.8370-8379.2004 [details]
    • Piette, A., Aarsman, M. E. G., Fraipont, C., den Blaauwen, T., Pastoret, S., & Nguyen-Disteche, M. (2004). Structural determinants required to target penicillin-binding protein 3 to the septum of Escherichia coli. Journal of Bacteriology, 186, 6110-6117. https://doi.org/10.1128/JB.186.18.6110-6117.2004 [details]
    • Sijbrandi, R., den Blaauwen, T., Tame, J. R. H., Oudega, B. R., Luirink, J., & Otto, B. R. (2004). Characterization of an iron-regulated alpha-enolase of Bacteroides fragilis. Microbes and infection, 7, 9-18. https://doi.org/10.1016/j.micinf.2004.09.013 [details]

    2003

    • den Blaauwen, T., Aarsman, M. E. G., Vischer, N. O. E., & Nanninga, N. (2003). Penicillin-binding protein PBP2 of Escherichia coli localizes preferentially at thge lateral wall and at mid cell in comparison with the old cell pole. Molecular Microbiology, 47, 539-547. https://doi.org/10.1046/j.1365-2958.2003.03316.x [details]

    2002

    • Scheffers, D-J., Wit, J. G., den Blaauwen, T., & Driessen, A. J. M. (2002). GTP Hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers. Biochemistry, 41, 521-529. https://doi.org/10.1021/bi011370i [details]

    2001

    2000

    2012

    2001

    • den Blaauwen, T., Nanninga, N., & Koomen, G. J. (2001). InhibitionFtsZ protein (de)polymerization.

    2000

    • den Blaauwen, T., Nanninga, N., & Koomen, G. J. (2000). Development of Antibacterial Agents via Inhibition of FtsZ (de)polymerisation.
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  • Ancillary activities
    • No ancillary activities