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How tetraspanin-mediated cell entry of SARS-CoV-2 can dysregulate the shedding of the ACE2 receptor by ADAM17.
Healy, Eamonn F.
  • Healy EF; Department of Chemistry, St. Edward's University, Austin, TX, 78704, USA. Electronic address: healy@stedwards.edu.
Biochem Biophys Res Commun ; 593: 52-56, 2022 02 19.
Article in English | MEDLINE | ID: covidwho-1633160
ABSTRACT
COVID-19, the respiratory infection caused by the novel coronavirus SARS-CoV-2, presents a clinical picture consistent with the dysregulation of many of the pathways mediated by the metalloprotease ADAM17. ADAM17 is a sheddase that plays a key role in the modulation of ACE2, the receptor which also functions as the point of attachment leading to cell entry by the virus. This work investigates the possibility that ADAM17 dysregulation and attachment of the SARS-CoV-2 virion to the ACE2 receptor are linked events, with the latter causing the former. Tetraspanins, the transmembrane proteins that function as scaffolds for the construction of viral entry platforms, are mooted as key components in this connection.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Virus Internalization / Tetraspanin 29 / ADAM17 Protein / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Observational study / Prognostic study Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Receptors, Virus / Virus Internalization / Tetraspanin 29 / ADAM17 Protein / Angiotensin-Converting Enzyme 2 / SARS-CoV-2 Type of study: Observational study / Prognostic study Limits: Humans Language: English Journal: Biochem Biophys Res Commun Year: 2022 Document Type: Article