The nucleocapsid protein of measles virus blocks host interferon response.

Virology

Laboratory Animal Research Center, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.

Published: March 2012

AI Article Synopsis

  • Measles virus (MV), part of the Morbillivirus genus, inhibits the host's immune response by interfering with interferon (IFN) signaling pathways.
  • Recent studies confirmed that the MV's P gene products affect these pathways, while the N protein also serves as a strong antagonist against IFN-α/β and γ.
  • The research revealed that MV-N blocks the nuclear import of activated STAT proteins, which is crucial for the inhibition of the IFN signaling, indicating that this property is common among other morbilliviruses as well.

Article Abstract

Measles virus (MV) belongs to the genus Morbillivirus of the family Paramyxoviridae. A number of paramyxoviruses inhibit host interferon (IFN) signaling pathways in host immune systems by various mechanisms. Inhibition mechanisms have been described for many paramyxoviruses. Although there are inconsistencies among previous reports concerning MV, it appears that P/V/C proteins interfere with the pathways. In this study, we confirmed the effects of MV P gene products of a wild MV strain on IFN pathways and examined that of other viral proteins on it. Interestingly, we found that N protein acts as an IFN-α/β and γ-antagonist as strong as P gene products. We further investigated the mechanisms of MV-N inhibition, and revealed that MV-N blocks the nuclear import of activated STAT without preventing STAT and Jak activation or STAT degradation, and that the nuclear translocation of MV-N is important for the inhibition. The inhibitory effect of the N protein was observed as a common feature of other morbilliviruses. The results presented in this report suggest that N protein of MV as well as P/V/C proteins is involved in the inhibition of host IFN signaling pathways.

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Source
http://dx.doi.org/10.1016/j.virol.2011.12.011DOI Listing

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