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    Evidence of Structural Protein Damage and Membrane Lipid Remodeling in Red Blood Cells from COVID-19 Patients

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    Author
    Thomas, Tiffany
    Stefanoni, Davide
    Dzieciatkowska, Monika
    Issaian, Aaron
    Nemkov, Travis
    Hill, Ryan C
    Francis, Richard O
    Hudson, Krystalyn E
    Buehler, Paul W
    Zimring, James C
    Hod, Eldad A
    Hansen, Kirk C
    Spitalnik, Steven L
    D'Alessandro, Angelo
    Show allShow less

    Date
    2020-10-26
    Journal
    Journal of Proteome Research
    Publisher
    American Chemical Society
    Type
    Article
    
    Metadata
    Show full item record
    See at
    https://doi.org/10.1021/acs.jproteome.0c00606
    Abstract
    The SARS-CoV-2 beta coronavirus is the etiological driver of COVID-19 disease, which is primarily characterized by shortness of breath, persistent dry cough, and fever. Because they transport oxygen, red blood cells (RBCs) may play a role in the severity of hypoxemia in COVID-19 patients. The present study combines state-of-the-art metabolomics, proteomics, and lipidomics approaches to investigate the impact of COVID-19 on RBCs from 23 healthy subjects and 29 molecularly diagnosed COVID-19 patients. RBCs from COVID-19 patients had increased levels of glycolytic intermediates, accompanied by oxidation and fragmentation of ankyrin, spectrin beta, and the N-terminal cytosolic domain of band 3 (AE1). Significantly altered lipid metabolism was also observed, in particular, short- and medium-chain saturated fatty acids, acyl-carnitines, and sphingolipids. Nonetheless, there were no alterations of clinical hematological parameters, such as RBC count, hematocrit, or mean corpuscular hemoglobin concentration, with only minor increases in mean corpuscular volume. Taken together, these results suggest a significant impact of SARS-CoV-2 infection on RBC structural membrane homeostasis at the protein and lipid levels. Increases in RBC glycolytic metabolites are consistent with a theoretically improved capacity of hemoglobin to off-load oxygen as a function of allosteric modulation by high-energy phosphate compounds, perhaps to counteract COVID-19-induced hypoxia. Conversely, because the N-terminus of AE1 stabilizes deoxyhemoglobin and finely tunes oxygen off-loading and metabolic rewiring toward the hexose monophosphate shunt, RBCs from COVID-19 patients may be less capable of responding to environmental variations in hemoglobin oxygen saturation/oxidant stress when traveling from the lungs to peripheral capillaries and vice versa.
    Keyword
    AE1
    SARS-CoV-2
    band 3
    erythrocyte
    lipidomics
    metabolomics
    proteomics
    Identifier to cite or link to this item
    http://hdl.handle.net/10713/14121
    ae974a485f413a2113503eed53cd6c53
    10.1021/acs.jproteome.0c00606
    Scopus Count
    Collections
    UMB Coronavirus Publications
    UMB Open Access Articles 2020

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