Berlin 2015 – scientific programme
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BP: Fachverband Biologische Physik
BP 17: Posters: Protein structure and dynamics
BP 17.7: Poster
Monday, March 16, 2015, 17:30–19:30, Poster A
Multivalent interaction of hemagglutinin with sialic acid as studied by scanning force microscopy and force spectroscopy — •Valentin Reiter1, Manuel Gensler1, Sumati Bhatia2, Luis Cuellar2, Daniel Lauster3, Rainer Haag2, Andreas Herrmann2, and Jürgen P. Rabe1 — 1Department of Physics, Humboldt-Universität zu Berlin — 2Institute of Chemistry & Biochemistry, Freie Universität Berlin — 3Department of Biology, Humboldt-Universität zu Berlin
The glycoprotein hemagglutinin (HA) is a transmembrane protein of the influenza virus that comprises over 80% of the envelope proteins present in the virus particle and accounts for the primary attachment of the virion to a target cell. The attachment happens due to hydrogen bonds between the three binding pockets of the HA globular domain and sialic acid (SA) molecules on the biological cell surface. The development of efficient inhibitors of virus binding requires precise knowledge of this interaction. On protein immobilizing surfaces the scanning force microscope (SFM) can be used to directly probe the bond strength of single and multiple HA - SA - interactions. SFM images are used to determine the surface density of the immobilized proteins. Then, single molecule force spectroscopy with cantilevers functionalized with SA is employed to measure the rupture forces between HA-SA bonds. The dissociation behavior is calculated from the distribution of rupture forces at various pulling speeds.