Influenza virus inhibits RNA polymerase II elongation

Virology. 2006 Jul 20;351(1):210-7. doi: 10.1016/j.virol.2006.03.005. Epub 2006 Apr 19.

Abstract

The influenza virus RNA-dependent RNA polymerase interacts with the serine-5 phosphorylated carboxy-terminal domain (CTD) of the large subunit of RNA polymerase II (Pol II). It was proposed that this interaction allows the viral RNA polymerase to gain access to host mRNA-derived capped RNA fragments required as primers for the initiation of viral mRNA synthesis. Here, we show, using a chromatin immunoprecipitation (ChIP) analysis, that similar amounts of Pol II associate with Pol II promoter DNAs in influenza virus-infected and mock-infected cells. However, there is a statistically significant reduction in Pol II densities in the coding region of Pol II genes in infected cells. Thus, influenza virus specifically interferes with Pol II elongation, but not Pol II initiation. We propose that influenza virus RNA polymerase, by binding to the CTD of initiating Pol II and subsequent cleavage of the capped 5' end of the nascent transcript, triggers premature Pol II termination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatin Immunoprecipitation
  • HeLa Cells
  • Humans
  • Influenza A virus / enzymology
  • Influenza A virus / physiology*
  • Protein Binding
  • RNA Polymerase II / metabolism*
  • RNA-Dependent RNA Polymerase / metabolism
  • Transcription, Genetic*

Substances

  • RNA Polymerase II
  • RNA-Dependent RNA Polymerase