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SARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide and boosts proinflammatory activity

View ORCID ProfileGanna Petruk, View ORCID ProfileManoj Puthia, View ORCID ProfileJitka Petrlova, Ann-Charlotte Strömdahl, Sven Kjellström, View ORCID ProfileArtur Schmidtchen
doi: https://doi.org/10.1101/2020.06.29.175844
Ganna Petruk
aDivision of Dermatology and Venereology, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
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Manoj Puthia
aDivision of Dermatology and Venereology, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
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Jitka Petrlova
aDivision of Dermatology and Venereology, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
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Ann-Charlotte Strömdahl
aDivision of Dermatology and Venereology, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
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Sven Kjellström
bDivision of Mass Spectrometry, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
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Artur Schmidtchen
aDivision of Dermatology and Venereology, Department of Clinical Sciences, Lund University, SE-22184 Lund, Sweden
cCopenhagen Wound Healing Center, Bispebjerg Hospital, Department of Biomedical Sciences, University of Copenhagen, DK-2400 Copenhagen, Denmark
dDermatology, Skåne University Hospital, SE-22185 Lund, Sweden
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  • For correspondence: artur.schmidtchen@med.lu.se
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ABSTRACT

There is a well-known and established link between high lipopolysaccharide (LPS) levels in blood and the metabolic syndrome (MS). MS is a risk factor for developing severe COVID-19 and acute respiratory distress syndrome (ARDS). Here we define an interaction between SARS-CoV-2 Spike (S) protein and LPS and its link to aggravated inflammation in vitro and in vivo. Electrophoresis under native conditions demonstrated that SARS-CoV-2 S protein binds to Escherichia coli LPS, forming high molecular weight aggregates. Microscale thermophoresis analysis further defined the interaction, having a KD of ~47 nM, similar to the observed affinity between LPS and the human receptor CD14. Moreover, S protein, when combined with low levels of LPS, boosted nuclear factor-kappa B (NF-κB) and cytokine responses in monocytic THP-1 cells and human blood, respectively. In an experimental model of localized inflammation, employing NF-κB reporter mice and in vivo bioimaging, S protein in conjunction with LPS significantly increased the inflammatory response when compared with S protein and LPS alone. Apart from providing information on LPS as a ligand for S protein, our results are of relevance for studies on comorbidities involving bacterial endotoxins, such as the MS, or co-existing acute and chronic infections in COVID-19 patients.

Competing Interest Statement

A.S is a founder and shareholder of in2cure AB, a company developing therapies based on host defense peptides. A patent application related to the present work, with A.S. and G.P. listed as inventors, has been filed.

  • Abbreviations

    ARDS
    acute respiratory distress syndrome
    COVID-19
    coronavirus disease 2019
    MS
    metabolic syndrome
    LBP
    LPS-binding protein
    LPS
    lipopolysaccharide
    NF-κB
    nuclear factor-kappa B
    SARS-CoV-2 Spike protein
    S protein
    TLR4
    Toll-like receptor 4
  • 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 June 29, 2020.
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    SARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide and boosts proinflammatory activity
    Ganna Petruk, Manoj Puthia, Jitka Petrlova, Ann-Charlotte Strömdahl, Sven Kjellström, Artur Schmidtchen
    bioRxiv 2020.06.29.175844; doi: https://doi.org/10.1101/2020.06.29.175844
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    SARS-CoV-2 Spike protein binds to bacterial lipopolysaccharide and boosts proinflammatory activity
    Ganna Petruk, Manoj Puthia, Jitka Petrlova, Ann-Charlotte Strömdahl, Sven Kjellström, Artur Schmidtchen
    bioRxiv 2020.06.29.175844; doi: https://doi.org/10.1101/2020.06.29.175844

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