I(nsp1)ecting SARS-CoV-2-ribosome interactions

Commun Biol. 2021 Jun 10;4(1):715. doi: 10.1038/s42003-021-02265-0.


While SARS-CoV-2 is causing modern human history's most serious health crisis and upending our way of life, clinical and basic research on the virus is advancing rapidly, leading to fascinating discoveries. Two studies have revealed how the viral virulence factor, nonstructural protein 1 (Nsp1), binds human ribosomes to inhibit host cell translation. Here, we examine the main conclusions on the molecular activity of Nsp1 and its role in suppressing innate immune responses. We discuss different scenarios potentially explaining how the viral RNA can bypass its own translation blockage and speculate on the suitability of Nsp1 as a therapeutic target.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 5' Untranslated Regions
  • Gene Expression Regulation, Viral
  • Host-Pathogen Interactions / physiology*
  • Humans
  • Immunity, Innate
  • Protein Biosynthesis
  • RNA, Messenger / metabolism
  • Ribosomes / metabolism
  • Ribosomes / virology*
  • SARS-CoV-2 / genetics
  • SARS-CoV-2 / pathogenicity*
  • Viral Nonstructural Proteins / chemistry
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*


  • 5' Untranslated Regions
  • NSP1 protein, SARS-CoV-2
  • RNA, Messenger
  • Viral Nonstructural Proteins