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Cell Membrane Derived Platform To Study Virus Binding Kinetics and Diffusion with Single Particle Sensitivity

Journal article
Authors N. Peerboom
E. Schmidt
Edward Trybala
S. Block
Thomas Bergström
H. P. Pace
M. Bally
Published in Acs Infectious Diseases
Volume 4
Issue 6
Pages 944-953
ISSN 2373-8227
Publication year 2018
Published at Institute of Biomedicine, Department of Infectious Medicine
Pages 944-953
Language en
Keywords virus-membrane interactions, supported lipid bilayers, herpes simplex virus, binding kinetics, single particle tracking, biomimetic sensing platform, herpes-simplex-virus, supported lipid-bilayers, type-1 glycoprotein-c, heparan-sulfate, protein mobility, hiv-1 particles, live cells, infection, receptor, fusion, Pharmacology & Pharmacy, Infectious Diseases, keuchi y, 1992, journal of biological chemistry, v267, p14685, sai ur, 1993, biochemistry, v32, p8140
Subject categories Infectious Medicine


Discovery and development of new antiviral therapies essentially rely on two key factors: an in-depth understanding of the mechanisms involved in viral infection and the development of fast and versatile drug screening platforms. To meet those demands, we present a biosensing platform to probe virus-cell membrane interactions on a single particle level. Our method is based on the formation of supported lipid bilayers from cell membrane material. Using total internal reflection fluorescence microscopy, we report the contribution of viral and cellular components to the interaction kinetics of herpes simplex virus type 1 with the cell membrane. Deletion of glycoprotein C (gC), the main viral attachment glycoprotein, or deletion of heparan sulfate, an attachment factor on the cell membrane, leads to an overall decrease in association of virions to the membrane and faster dissociation from the membrane. In addition to this, we perform binding inhibition studies using the antiviral compound heparin to estimate its IC50 value. Finally, single particle tracking is used to characterize the diffusive behavior of the virus particles on the supported lipid bilayers. Altogether, our results promote this platform as a complement to existing bioanalytical assays, being at the interface between simplified artificial membrane models and live cell experiments.

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