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

Shinji Ohno, Nobuyuki Ono, Makoto Takeda, Kaoru Takeuchi, Yusuke Yanagi

研究成果: Contribution to journalArticle査読

114 被引用数 (Scopus)

抄録

Interferon (IFN)-α and -β 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-α/β signalling. Here, the wild-type JC-B strain of MV was shown to grow comparably in the presence and absence of IFN-α, 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-α signalling. The V protein of the Edmonston strain from the ATCC also inhibited IFN-α 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-α 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-α 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-α 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.

本文言語英語
ページ(範囲)2991-2999
ページ数9
ジャーナルJournal of General Virology
85
10
DOI
出版ステータス出版済み - 10 2004

All Science Journal Classification (ASJC) codes

  • ウイルス学

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