Berlin 2018 – scientific programme
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BP: Fachverband Biologische Physik
BP 1: Protein Structure and Dynamics
BP 1.5: Talk
Monday, March 12, 2018, 10:45–11:00, H 1028
Characterisation of binding interaction of the influenza virus proteins Hemagglutinin and Neuraminidase with a synthetic sialic acid receptor by single molecule force spectroscopy — •Valentin Reiter-Scherer1, Sumati Bhatia2, Jose Luis Cuellar-Camacho2, Daniel Lauster1, Rainer Haag2, Andreas Herrmann1, and Jürgen P. Rabe1 — 1HU Berlin — 2FU Berlin
The influenza virus is causing annual epidemics. In the first step of the infection, the virion binds to a host cell through multivalent attachment, mediated by the major virus spike protein hemagglutinin (HA) and sialic acid (SA) receptors of the glycocalyx of epithelial cells of the respiratory tract [1]. Neuraminidase (NA) on the other hand is known to cleave SA from the glycoproteins enabling the release of newly formed virions. A common strategy to inhibit infection, is the use of drugs that bind specifically to the binding pockets of the viral proteins to prevent SA binding [2]. Here we introduce a ligand architecture (LAPEG-SA) ideally synthesized to test the tensile strength between individual SA units and recombinant HA and NA of influenza H1N1. Individual binding strength and affinity at the single molecular level, being of central importance for the development of novel potent inhibitors, are characterized by scanning force microscope based single molecule force spectroscopy. Rupture forces of the SA protein binding are measured for several rates of force loading and the dissociation parameters off-rate as well rupture length are derived from the single barrier model [3]. - [1] Sieben et al., PNAS 2012. [2] Bhatia et al., J. Am. Chem. Soc. 2016. [3] Evans et al., Biophys. Journal 1997.