Amelioration of SARS-CoV-2 infection by ANO6 phospholipid scramblase inhibition

Cell Rep. 2022 Jul 19;40(3):111117. doi: 10.1016/j.celrep.2022.111117. Epub 2022 Jul 4.

Abstract

As an enveloped virus, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) delivers its viral genome into host cells via fusion of the viral and cell membranes. Here, we show that ANO6/TMEM16F-mediated cell surface exposure of phosphatidylserine is critical for SARS-CoV-2 entry and that ANO6-selective inhibitors are effective against SARS-CoV-2 infections. Application of the SARS-CoV-2 Spike pseudotyped virus (SARS2-PsV) evokes a cytosolic Ca2+ elevation and ANO6-dependent phosphatidylserine externalization in ACE2/TMPRSS2-positive mammalian cells. A high-throughput screening of drug-like chemical libraries identifies three different structural classes of chemicals showing ANO6 inhibitory effects. Among them, A6-001 displays the highest potency and ANO6 selectivity and it inhibits the single-round infection of SARS2-PsV in ACE2/TMPRSS2-positive HEK 293T cells. More importantly, A6-001 strongly inhibits authentic SARS-CoV-2-induced phosphatidylserine scrambling and SARS-CoV-2 viral replications in Vero, Calu-3, and primarily cultured human nasal epithelial cells. These results provide mechanistic insights into the viral entry process and offer a potential target for pharmacological intervention to protect against coronavirus disease 2019 (COVID-19).

Keywords: ANO6/TMEM16F; CP: Microbiology; SARS-CoV-2; phosphatidylserine; virus-cell fusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiotensin-Converting Enzyme 2
  • Animals
  • Anoctamins
  • COVID-19 Drug Treatment*
  • Humans
  • Mammals / metabolism
  • Phosphatidylserines
  • Phospholipid Transfer Proteins / metabolism
  • SARS-CoV-2
  • Virus Internalization

Substances

  • ANO6 protein, human
  • Anoctamins
  • Phosphatidylserines
  • Phospholipid Transfer Proteins
  • Angiotensin-Converting Enzyme 2