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SARS-CoV-2 Accessory Protein ORF8 Decreases Antibody-Dependent Cellular Cytotoxicity.

Guillaume Beaudoin-Bussières1,2, Ariana Arduini3,4, Catherine Bourassa1

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SARS-CoV-2 ORF8 protein binds immune cells, reducing antibody-dependent cellular cytotoxicity (ADCC). This viral immune evasion strategy helps the virus escape host humoral responses.

Keywords:
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Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • SARS-CoV-2 utilizes diverse immune evasion strategies, including Spike protein mutations and accessory proteins.
  • The accessory protein ORF8 is rapidly evolving and implicated in modulating disease severity.
  • Understanding ORF8's role in immune evasion is crucial for comprehending SARS-CoV-2 pathogenesis.

Purpose of the Study:

  • To investigate the effect of the SARS-CoV-2 ORF8 protein on peripheral blood mononuclear cells (PBMCs).
  • To elucidate the mechanism by which ORF8 contributes to viral immune evasion.

Main Methods:

  • Studied the interaction of ORF8 with human PBMCs, including monocytes and NK cells.
  • Quantified ORF8 binding affinity to CD16a (FcγRIIIA) using nanomolar affinity measurements.
  • Assessed the impact of ORF8 on cell surface CD16 expression and antibody-dependent cellular cytotoxicity (ADCC) capacity.

Main Results:

  • ORF8 protein binds to monocytes and NK cells within PBMCs.
  • ORF8 exhibits high-affinity binding to CD16a (FcγRIIIA).
  • ORF8 reduces surface CD16 levels on monocytes and NK cells, significantly impairing ADCC.

Conclusions:

  • Identified a novel immune evasion mechanism for SARS-CoV-2 involving ORF8.
  • ORF8 actively suppresses antibody-dependent cellular cytotoxicity (ADCC), a key component of humoral immunity.
  • This finding highlights ORF8's role in SARS-CoV-2's ability to evade host immune responses.