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Fungal and Parasitic Infections

Large-Scale Investigation of Leishmania Interaction Networks with Host Extracellular Matrix by Surface Plasmon Resonance Imaging

Marie Fatoux-Ardore, Franck Peysselon, Anthony Weiss, Patrick Bastien, Francine Pratlong, Sylvie Ricard-Blum
J. L. Flynn, Editor
Marie Fatoux-Ardore
aUMR 5086 CNRS—Université Lyon 1, Institut de Biologie et Chimie des Protéines, Lyon, France
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Franck Peysselon
aUMR 5086 CNRS—Université Lyon 1, Institut de Biologie et Chimie des Protéines, Lyon, France
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Anthony Weiss
bSchool of Molecular Bioscience, University of Sydney, NSW, Australia
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Patrick Bastien
cUniversité Montpellier 1, Centre National de Référence des Leishmanioses, UMR MIVEGEC (CNRS 5290, IRD 224, UM1, UM2), Département de Parasitologie-Mycologie, CHRU de Montpellier, Montpellier, France
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Francine Pratlong
cUniversité Montpellier 1, Centre National de Référence des Leishmanioses, UMR MIVEGEC (CNRS 5290, IRD 224, UM1, UM2), Département de Parasitologie-Mycologie, CHRU de Montpellier, Montpellier, France
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Sylvie Ricard-Blum
aUMR 5086 CNRS—Université Lyon 1, Institut de Biologie et Chimie des Protéines, Lyon, France
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J. L. Flynn
Roles: Editor
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DOI: 10.1128/IAI.01146-13
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This article has a correction. Please see:

  • Large-Scale Investigation of Leishmania Interaction Networks with Host Extracellular Matrix by Surface Plasmon Resonance Imaging
    - March 19, 2014

ABSTRACT

We have set up an assay to study the interactions of live pathogens with their hosts by using protein and glycosaminoglycan arrays probed by surface plasmon resonance imaging. We have used this assay to characterize the interactions of Leishmania promastigotes with ∼70 mammalian host biomolecules (extracellular proteins, glycosaminoglycans, growth factors, cell surface receptors). We have identified, in total, 27 new partners (23 proteins, 4 glycosaminoglycans) of procyclic promastigotes of six Leishmania species and 18 partners (15 proteins, 3 glycosaminoglycans) of three species of stationary-phase promastigotes for all the strains tested. The diversity of the interaction repertoires of Leishmania parasites reflects their dynamic and complex interplay with their mammalian hosts, which depends mostly on the species and strains of Leishmania. Stationary-phase Leishmania parasites target extracellular matrix proteins and glycosaminoglycans, which are highly connected in the extracellular interaction network. Heparin and heparan sulfate bind to most Leishmania strains tested, and 6-O-sulfate groups play a crucial role in these interactions. Numerous Leishmania strains bind to tropoelastin, and some strains are even able to degrade it. Several strains interact with collagen VI, which is expressed by macrophages. Most Leishmania promastigotes interact with several regulators of angiogenesis, including antiangiogenic factors (endostatin, anastellin) and proangiogenic factors (ECM-1, VEGF, and TEM8 [also known as anthrax toxin receptor 1]), which are regulated by hypoxia. Since hypoxia modulates the infection of macrophages by the parasites, these interactions might influence the infection of host cells by Leishmania.

FOOTNOTES

    • Received 10 September 2013.
    • Returned for modification 9 October 2013.
    • Accepted 13 November 2013.
    • Accepted manuscript posted online 25 November 2013.
  • Supplemental material for this article may be found at http://dx.doi.org/10.1128/IAI.01146-13.

  • Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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Large-Scale Investigation of Leishmania Interaction Networks with Host Extracellular Matrix by Surface Plasmon Resonance Imaging
Marie Fatoux-Ardore, Franck Peysselon, Anthony Weiss, Patrick Bastien, Francine Pratlong, Sylvie Ricard-Blum
Infection and Immunity Jan 2014, 82 (2) 594-606; DOI: 10.1128/IAI.01146-13

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Large-Scale Investigation of Leishmania Interaction Networks with Host Extracellular Matrix by Surface Plasmon Resonance Imaging
Marie Fatoux-Ardore, Franck Peysselon, Anthony Weiss, Patrick Bastien, Francine Pratlong, Sylvie Ricard-Blum
Infection and Immunity Jan 2014, 82 (2) 594-606; DOI: 10.1128/IAI.01146-13
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