Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection

Nat Chem Biol. 2023 Mar;19(3):275-283. doi: 10.1038/s41589-022-01149-6. Epub 2022 Sep 29.

Abstract

Prevention of infection and propagation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a high priority in the Coronavirus Disease 2019 (COVID-19) pandemic. Here we describe S-nitrosylation of multiple proteins involved in SARS-CoV-2 infection, including angiotensin-converting enzyme 2 (ACE2), the receptor for viral entry. This reaction prevents binding of ACE2 to the SARS-CoV-2 spike protein, thereby inhibiting viral entry, infectivity and cytotoxicity. Aminoadamantane compounds also inhibit coronavirus ion channels formed by envelope (E) protein. Accordingly, we developed dual-mechanism aminoadamantane nitrate compounds that inhibit viral entry and, thus, the spread of infection by S-nitrosylating ACE2 via targeted delivery of the drug after E protein channel blockade. These non-toxic compounds are active in vitro and in vivo in the Syrian hamster COVID-19 model and, thus, provide a novel avenue to pursue therapy.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Angiotensin-Converting Enzyme 2 / metabolism
  • COVID-19*
  • Humans
  • Peptidyl-Dipeptidase A / metabolism
  • Protein Binding
  • SARS-CoV-2 / metabolism

Substances

  • spike protein, SARS-CoV-2
  • Angiotensin-Converting Enzyme 2
  • Peptidyl-Dipeptidase A