Inhibition of cellular RNA methyltransferase abrogates influenza virus capping and replication

Science. 2023 Feb 10;379(6632):586-591. doi: 10.1126/science.add0875. Epub 2023 Feb 9.

Abstract

Orthomyxo- and bunyaviruses steal the 5' cap portion of host RNAs to prime their own transcription in a process called "cap snatching." We report that RNA modification of the cap portion by host 2'-O-ribose methyltransferase 1 (MTr1) is essential for the initiation of influenza A and B virus replication, but not for other cap-snatching viruses. We identified with in silico compound screening and functional analysis a derivative of a natural product from Streptomyces, called trifluoromethyl-tubercidin (TFMT), that inhibits MTr1 through interaction at its S-adenosyl-l-methionine binding pocket to restrict influenza virus replication. Mechanistically, TFMT impairs the association of host cap RNAs with the viral polymerase basic protein 2 subunit in human lung explants and in vivo in mice. TFMT acts synergistically with approved anti-influenza drugs.

MeSH terms

  • A549 Cells
  • Alphainfluenzavirus* / drug effects
  • Animals
  • Antiviral Agents* / chemistry
  • Antiviral Agents* / pharmacology
  • Betainfluenzavirus* / drug effects
  • Biological Products* / chemistry
  • Biological Products* / pharmacology
  • Computer Simulation
  • Enzyme Inhibitors* / chemistry
  • Enzyme Inhibitors* / pharmacology
  • Humans
  • Methyltransferases* / antagonists & inhibitors
  • Mice
  • RNA Caps* / metabolism
  • RNA, Messenger / metabolism
  • RNA, Viral / biosynthesis
  • Streptomyces / chemistry
  • Tubercidin* / analogs & derivatives
  • Tubercidin* / pharmacology
  • Virus Replication* / drug effects

Substances

  • RNA Caps
  • RNA, Messenger
  • RNA, Viral
  • Biological Products
  • Antiviral Agents
  • Tubercidin
  • CMTR1 protein, human
  • Methyltransferases
  • Enzyme Inhibitors