Regensburg 2016 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 23: Posters - Protein Structure and Dynamics

BP 23.4: Poster

Montag, 7. März 2016, 17:30–19:30, Poster C

Dissociation dynamics of the viral protein hemagglutinin and the cellular receptor sialic acid analyzed by single-molecule force spectroscopy — •Valentin Reiter1, Sumati Bhatia2, Daniel Lauster3, Manuel Gensler1, Luis Cuellar2, Rainer Haag2, Andreas Herrmann3, and Jürgen P. Rabe11Department of Physics + IRIS Adlershof, Humboldt-Universität zu Berlin — 2Department of Chemistry, Freie Universität Berlin — 3Department of Biology, Humboldt-Universität zu Berlin

The trimeric transmembrane protein hemagglutinin (HA) comprises over 80% of the envelope proteins present in the influenza virus and it has an essential role in the reproduction of the virus in epithelial cells by binding to sialic acid (SA) containing glycoproteins [1]. Binding of nanoparticles to the HA can hinder cell attachment and inhibit viral infection [2]. For the development of more potent inhibitors, the binding should be understood on the single-molecule level. Scanning force microscope (SFM) based single-virion force spectroscopy has proven to be a valuable tool to directly probe molecular interactions of virion-cell binding and precisely determine pN-ranged forces that govern the receptor ligand dissociation [3]. Using immobilized single proteins and SFM cantilevers functionalized with SA we measured the rupture forces of single HA-SA bonds under dynamic loads and derive a significantly larger dissociation rate and rupture length compared to single virion experiments [3] which will be discussed. [1] G. M. Whitesides et al., Angew. Chem. Int. Ed. 1998, 37, 2754; [2] I. Papp et al., ChemBioChem 2011, 12, 887; [3] C. Sieben et al., PNAS, 2012, 109, 13626.

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