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Apicomplexan F-actin is required for efficient nuclear entry during host cell invasion

Mario Del Rosario, Javier Periz, Georgios Pavlou, Oliver Lyth, Fernanda Latorre-Barragan, Sujaan Das, Gurman S. Pall, Johannes Felix Stortz, Leandro Lemgruber, Jake Baum, View ORCID ProfileIsabelle Tardieux, Markus Meissner
doi: https://doi.org/10.1101/646463
Mario Del Rosario
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Javier Periz
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Georgios Pavlou
4Institute for Advanced Biosciences, CNRS UMR5309, INSERM U1209, Université Grenoble Alpes, Grenoble, 38700, France.
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Oliver Lyth
3Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, UK.
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Fernanda Latorre-Barragan
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
5Faculty of Science, Food Engineering and 20 Biotechnology, Technical University of Ambato, Ambato, Ecuador.
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Sujaan Das
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Gurman S. Pall
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Johannes Felix Stortz
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Leandro Lemgruber
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
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Jake Baum
3Department of Life Sciences, Imperial College London, South Kensington, London SW7 2AZ, UK.
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Isabelle Tardieux
4Institute for Advanced Biosciences, CNRS UMR5309, INSERM U1209, Université Grenoble Alpes, Grenoble, 38700, France.
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  • ORCID record for Isabelle Tardieux
Markus Meissner
1Wellcome Centre For Molecular Parasitology, Institute of Infection, Immunity & Inflammation, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA.
2Lehrstuhl für experimentelle Parasitologie, Ludwig-Maximilians-Universität, LMU, Tierärztliche Fakultät, Leopoldstr. 5, 80802 München, Germany.
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  • For correspondence: Markus.Meissner@lmu.de
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Abstract

The obligate intracellular parasites Toxoplasma gondii and Plasmodium spp. invade host cells by injecting a protein complex into the membrane of the targeted cell that bridges the two cells through the assembly of a ring-like junction. This circular junction stretches while the parasites applies a traction force to pass through; a step that typically concurs with transient constriction of the parasite body. Here we show that the junction can oppose resistance to the passage of the parasite’s nucleus. Super-resolution microscopy and real time imaging highlighted an F-actin pool at the apex of pre-invading parasite, an F-actin ring at the junction area during invasion but also networks of perinuclear and posteriorly localized F-actin. Mutant parasites with dysfunctional acto-myosin showed significant decrease of junctional and perinuclear F-actin and are coincidently affected in nuclear passage through the junction. We propose that the F-actin machinery eases nuclear passage by stabilising the junction and pushing the nucleus through the constriction, providing first evidence for a dual contribution of actin-forces during host cell invasion by apicomplexan parasites.

Footnotes

  • Abbreviation: CD Cytochalasin-D, CLEM corelative light and electron microscopy, TJ tight junctional ring, SR-SIM Super Resolution – Structure Illumination Microscopy, Cb Chromobody, FP Fluorescent protein

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted May 23, 2019.
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Apicomplexan F-actin is required for efficient nuclear entry during host cell invasion
Mario Del Rosario, Javier Periz, Georgios Pavlou, Oliver Lyth, Fernanda Latorre-Barragan, Sujaan Das, Gurman S. Pall, Johannes Felix Stortz, Leandro Lemgruber, Jake Baum, Isabelle Tardieux, Markus Meissner
bioRxiv 646463; doi: https://doi.org/10.1101/646463
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Apicomplexan F-actin is required for efficient nuclear entry during host cell invasion
Mario Del Rosario, Javier Periz, Georgios Pavlou, Oliver Lyth, Fernanda Latorre-Barragan, Sujaan Das, Gurman S. Pall, Johannes Felix Stortz, Leandro Lemgruber, Jake Baum, Isabelle Tardieux, Markus Meissner
bioRxiv 646463; doi: https://doi.org/10.1101/646463

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