CRC 765/3: Characterization and Optimization and Action Principle: New Architectures, Functions and Applications (SP C06)

The goal of the project is the inhibition of fusion properties of influenza viruses by means of a specific interaction of multivalent ligands with the fusion protein hemagglutinin. By using multivalent ligands the principles of an amplification mechanism will be unravelled. To this end, nanoparticles covered with those ligands will be used. Several methods including imaging techniques will be applied to study the mechanism and the underlying interaction between ligand and hemagglutinin. Strategies for efficient inhibition of virus infection will suggested.

Principal Investigators
Herrmann, Andreas Prof. Dr. rer. nat. (Details) (Molecular Biophysics)

Participating external organizations

Duration of Project
Start date: 01/2008
End date: 12/2019

Research Areas
angewandte Mathematik, Biologie, Chemie, Medizin, Physik

SFB 765
Sieben, C., Kappel, C., Zhu, R., Wozniak, A., Rankl, C., Hinterdorfer, P., Grubmüller, H., Herrmann, A. (2012) Influenza virus binds its host cell using multiple dynamic interactions. Proc Natl Acad Sci U S A. 109:13626-13631

Schade, M., Knoll, A., Vogel, A., Seitz, O., Liebscher, J., Huster, D., Herrmann, A., Arbuzova, A. (2012) Remote control of lipophilic nucleic acids domain partitioning by DNA hybridization and enzymatic cleavage. JACS 134, 20490-20497

Heek, T., Nikolaus, J., Schwarzer, R., Fasting, C., Welker, P., Licha, K., Herrmann, A., Haag, R. (2013) An amphiphilic perylene imido diester for selective cellular imaging. Bioconj. Chem. 24,153-158.

Beutel, O., Nikolaus, J., Birkholz, O., You, C., Schmidt, T., Herrmann, A., Piehler, J. (2013) High-fidelity protein targeting into membrane lipid microdomains in living cells. Angewandte Chem. Internat. Ed. 53, 1311-1315

Vonnemann, J., Sieben, C., Wolff, C., Ludwig, K., Böttcher, C., Herrmann, A., Haag, R. (2014) Virus inhibition induced by polyvalent nanoparticles of different sizes. Nanoscale 6, 2353-2360

Li, S., Sieben, C., Ludwig, K., Herrmann, A., Eghiaian, F., Schaap, I.A.T. (2014) pH-controlled two-step uncoating of influenza virus. Biophys J. 106, 1447-1456

Mair, C., Sieben, C., Ludwig, K., Herrmann, A. (2014) Receptor Binding and pH stability - How Influenza A virus hemagglutinin affects host-specific virus infection. Biochim. Biophys. Acta 1838, 1153-1168

Serien, D., Grimm, C., Liebscher, J., Herrmann, A., Arbuzova, A. (2014) DNA-controlled aggregation of virus like particles – mimicking a tetherin-like mechanism. New J. Chem. 38, 5181-5185.

Lauster, D., Vazquez, O., Schwarzer, R., Seitz, O., Herrmann, A. (2015) Potential of proapoptotic peptides to induce formation of giant plasma membrane vesicles with lipid domain. ChemBioChem, 16,1288-92

Lauster, D., Pawolski, D., Julian Storm, J., Ludwig, K., Volkmer, R., Memczak, H., Herrmann, A., Bhatia, S. (2015) Potential of acylated peptides to target the influenza A virus. Beilstein J.Org. Chem., 11, 589-595.

Memczak, H., Lauster, D., Kar, P., Di Lella, S., Volkmer, R., Knecht, V., Herrmann, A., Ehrentreich-Förster, E., Bier, F.F., Stöcklein, W.F.M. (2016) Anti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus Binding, Plos One, 11(7):e0159074. doi: 10.1371/journal.pone.0159074. eCollection 2016.

Sieben, C., Herrmann, A. (2017) The ties that bind. Nature Nanotechnology 12, 102-103

Gholami, M.F., Lauster, D., Ludwig, K., Storm, J., Ziem, B., Severin, N., Böttcher, C., Rabe, J.P., Herrmann, A., Adeli, M., Haag, R. (2017) Functionalized Graphene as Extracellular Matrix Mimics: Toward Well-Defined 2D Nanomaterials for Multivalent Virus Interactions. Adv. Funct. Materials, DOI: 10.1002/adfm.201606477

Lauster, D., Glanz, M., Bardua, M., Ludwig, K., Hellmund, M., Hoffmann, U., Hamann, A., Böttcher, C., Haag, R., Hackenberger, C., Herrmann, A. (2017) Multivalent Peptide-Nanoparticle-conjugates for Influenza Virus Inhibition. Internat. Ed. Angewandte Chemie, 56, 5931-5936

Bhatia, S.*, Lauster, D.*, Bardua, M., Ludwig, K., Angioletti-Uberti, S., Popp, N., Hoffmann, U., Paulus, F., Budt, M., Stadtmüller, M., Wolff, T., Hamann, A., Böttcher, C, Herrmann, A.#, Haag, R.# (2017) Linear polysialoside outperforms dendritic analogs for inhibition of influenza virus infection in vitro and in vivo. Biomaterials 138, 22-34.

Bandlow, V., Liese, S., Lauster, D., Ludwig, K., Netz, R., Herrmann, A., Seitz, O. (2017) Spatial screening of hemagglutinin on Influenza A virus particles: Sialyl-LacNAc displays on DNA and PEG scaffolds reveal the requirements for bivalency enhanced interactions with weak monovalent binders. JACS, 139(45):16389-16397.

Donskyi, I, Drüke, M., Silberreis, K., Lauster, D., Ludwig, K., Kühne, C., Unger, W., Böttcher, C., Herrmann, A., Dernedde, J., Adeli, M, Haag R. (2018) Interactions of Fullerene-Polyglycerol Sulfates at Viral and Cellular Interfaces. Small Apr;14(17):e1800189. doi: 10.1002/smll.201800189.

Kiran, P., Bhatia, S., Lauster, D., Aleksić, S., Fleck, C., Peric, N., Maison, W., Liese, S., Keller, B.G., Herrmann, A., Haag, R. (2018) Exploring rigid and flexible core trivalent sialosides for influenza virus inhibition. Chemistry- A Europ. J., 24(72):19373-19385. doi: 10.1002/chem.201804826.

Bandlow, V., Lauster, D., Ludwig, K., Hilsch, M., Reiter-Scherer, V., Rabe, J.P., Böttcher, C., Herrmann, A., Seitz, O. (2019) Sialyl-LacNAc-PNA∙DNA concatamers by rolling circle amplification as multivalent inhibitors for Influenza A virus particles. ChemBioChem, 20(2):159-165. doi: 10.1002/cbic.201800643.

Reiter-Scherer, V., Cuellar-Camacho, J.L., Bhatia, S., Haag, R., Herrmann, A., Lauster, D., Rabe, J.P. (2019) Force spectroscopy shows dynamic binding of influenza hemagglutinin and neuraminidase to sialic acid. Biophys. J.,

Müller, M., Lauster, D., Wildenauer, H., Herrmann, A., Block, S. (2019) Mobility-based quantification of multivalent virus-receptor interactions: New insights into Influenza A virus binding mode. Nano Letters, 19(3):1875-1882. doi: 10.1021/acs.nanolett.8b04969. Epub 2019 Feb 13. PMID: 30719917

Anedchenko, E.A., Samel-Pommerencke, A., Nguyen, T.M.T., Shahnejat-Bushehri, S., Pöpsel, S.J., Lauster, D., Herrmann, A., Rappsilber, J., Cuomo, A., Bonaldi, T., Ehrenhofer-Murray, A. (2019) The kinetochore module Okp1CENP-Q/Ame1CENP-U is a reader for N-terminal modifications on the centromeric histone Cse4CENP-A. EMBO J. e98991,1-14

Klenk, S., Lauster, D., Ludwig, K., Nojoumi, S., Behren, S., Adam, L., Stadtmüller, M., Saenger, S., Zimmler, S., Höntzke, K., Ling, Y., Hoffmann, U., Bardua, M., Hamann, A., Witzenrath, M., Sander, L.E., Wolff, T., Hocke, A.C., Hippenstiel, S., De Carlo, S., Neudecker, J., Budisa, N., Netz, R.R., Böttcher, C., Liese, S., Herrmann, A., Hackenberger, C.P.R. (2020) Phage capsid nanoparticles with defined ligand arrangement block influenza virus entry Nature Nanotechnology, accepted

Last updated on 2021-14-07 at 15:13