Dissection of measles virus V protein in relation to its ability to block alpha/beta interferon signal transduction

J Gen Virol. 2004 Oct;85(Pt 10):2991-2999. doi: 10.1099/vir.0.80308-0.


Interferon (IFN)-alpha and -beta are the main cytokines for innate immune responses against viral infections. To replicate efficiently in the hosts, viruses have evolved various countermeasures to the IFN response. The V protein of measles virus (MV) has been shown to block IFN-alpha/beta signalling. Here, the wild-type IC-B strain of MV was shown to grow comparably in the presence and absence of IFN-alpha, whereas replication of the Edmonston tag strain recovered from cloned DNA was strongly suppressed in its presence. The V protein of the IC-B strain, but not the Edmonston tag strain, blocked IFN-alpha signalling. The V protein of the Edmonston strain from the ATCC also inhibited IFN-alpha signalling. There were three amino acid differences between the V proteins of the Edmonston ATCC and tag strains, and substitutions of both residues at positions 110 and 272 were required for the Edmonston ATCC V protein to lose IFN-antagonist activity. The P protein of the IC-B strain, which shares the N-terminal 231 aa residues with the V protein, also inhibited IFN-alpha signalling. Indeed, fragments comprising only those 231 residues of the IC-B and Edmonston ATCC V proteins, but not the Edmonston tag V protein, were able to block IFN-alpha signalling. However, the N-terminal region of the Edmonston tag V protein, when attached to the C-terminal region of the Edmonston ATCC V protein, inhibited IFN-alpha signalling. Taken together, our results indicate that both the N- and C-terminal regions contribute to the IFN-antagonist activity of the MV V protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chlorocebus aethiops
  • Interferon-alpha / antagonists & inhibitors*
  • Interferon-beta / antagonists & inhibitors*
  • Phosphoproteins / chemistry
  • Phosphoproteins / physiology*
  • Signal Transduction*
  • Structure-Activity Relationship
  • Vero Cells
  • Viral Proteins / chemistry
  • Viral Proteins / physiology*


  • Interferon-alpha
  • Phosphoproteins
  • V protein, measles virus
  • Viral Proteins
  • Interferon-beta