How tetraspanin-mediated cell entry of SARS-CoV-2 can dysregulate the shedding of the ACE2 receptor by ADAM17

Eamonn F Healy1

  • 1Department of Chemistry, St. Edward's University, Austin, TX, 78704, USA.

Insights

The novel coronavirus SARS-CoV-2 causes COVID-19, potentially by disrupting the metalloprotease ADAM17. This study explores if virus attachment to the ACE2 receptor triggers ADAM17 dysregulation, involving tetraspanins in viral entry.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • COVID-19 is a respiratory illness caused by SARS-CoV-2.
  • The metalloprotease ADAM17 is implicated in COVID-19 pathogenesis.
  • ADAM17 modulates ACE2, the SARS-CoV-2 cell entry receptor.

Purpose of the Study:

  • To investigate the link between SARS-CoV-2 attachment to ACE2 and ADAM17 dysregulation.
  • To explore the role of tetraspanins in forming viral entry platforms.

Main Methods:

  • This study proposes a hypothesis based on existing literature.
  • Further experimental validation is required.

Main Results:

  • The attachment of SARS-CoV-2 to ACE2 may cause ADAM17 dysregulation.
  • Tetraspanins are hypothesized to be crucial for viral entry platform assembly.

Conclusions:

  • ADAM17 dysregulation is a potential consequence of SARS-CoV-2 binding to ACE2.
  • Tetraspanins may facilitate SARS-CoV-2 cell entry by scaffolding viral entry platforms.

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