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Cellular Protrusions Engage Viral Infection Enhancing EF-C Peptide Nanofibrils

Desiree Schütz, Sascha Rode, Clarissa Read, Janis A. Müller, Bernhard Glocker, Konstantin Sparrer, Oliver Fackler, Paul Walther, Jan Münch
doi: https://doi.org/10.1101/2020.10.01.321810
Desiree Schütz
1Institute of Molecular Virology, Ulm University Medical Center, Ulm, 89081, Germany
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Sascha Rode
1Institute of Molecular Virology, Ulm University Medical Center, Ulm, 89081, Germany
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Clarissa Read
2Central Facility for Electron Microscopy, Ulm University, Ulm, 89081, Germany
3Institute of Virology, Ulm University Medical Center, Ulm, 89081, Germany
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Janis A. Müller
1Institute of Molecular Virology, Ulm University Medical Center, Ulm, 89081, Germany
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Bernhard Glocker
2Central Facility for Electron Microscopy, Ulm University, Ulm, 89081, Germany
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Konstantin Sparrer
1Institute of Molecular Virology, Ulm University Medical Center, Ulm, 89081, Germany
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Oliver Fackler
4Center for Integrative Infectious Disease Research, Integrative Virology, University Hospital Heidelberg, Germany; German Center for Infection Research (DZIF), Partner Site Heidelberg, Heidelberg 69120, Germany
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Paul Walther
2Central Facility for Electron Microscopy, Ulm University, Ulm, 89081, Germany
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Jan Münch
1Institute of Molecular Virology, Ulm University Medical Center, Ulm, 89081, Germany
5Core Facility Functional Peptidomics, Ulm University Medical Center, Ulm, 89081, Germany
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  • For correspondence: jan.muench@uni-ulm.de
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Abstract

Self-assembling peptide nanofibrils (PNF) have gained increasing attention as versatile molecules in material science and biomedicine. One important application of PNF is to enhance retroviral gene transfer, a technology that has been central to the development of gene therapy. The best-investigated and commercially available PNF is derived from a 12-mer peptide termed EF-C. The mechanism of transduction enhancement depends on the polycationic surface of EF-C PNF, which binds to the negatively charged membranes of viruses and cells thereby overcoming electrostatic repulsion and increasing virion attachment and fusion. Assuming an even distribution of charges at the surfaces of virions and cells would result in an evenly distributed interaction of the virions with the cell surface. However, we here report that PNF do not randomly bind at the cell surface but are actively engaged by cellular protrusions. Chemical suppression of protrusion formation in cell lines and primary CD4+ T cells greatly reduced fibril binding and hence virion binding. Thus, the mechanism of PNF-mediated viral transduction enhancement involves active engagement of virus-loaded fibrils by cellular protrusions.

Competing Interest Statement

Author J.M. is inventor of patents claiming to use EF-C PNF as transduction enhancer.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
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Posted October 01, 2020.
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Cellular Protrusions Engage Viral Infection Enhancing EF-C Peptide Nanofibrils
Desiree Schütz, Sascha Rode, Clarissa Read, Janis A. Müller, Bernhard Glocker, Konstantin Sparrer, Oliver Fackler, Paul Walther, Jan Münch
bioRxiv 2020.10.01.321810; doi: https://doi.org/10.1101/2020.10.01.321810
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Cellular Protrusions Engage Viral Infection Enhancing EF-C Peptide Nanofibrils
Desiree Schütz, Sascha Rode, Clarissa Read, Janis A. Müller, Bernhard Glocker, Konstantin Sparrer, Oliver Fackler, Paul Walther, Jan Münch
bioRxiv 2020.10.01.321810; doi: https://doi.org/10.1101/2020.10.01.321810

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