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Journal of Virology, August 2000, p. 7064-7071, Vol. 74, No. 15
Laboratoire de Virologie et Immunologie
Moléculaires INRA, C.R.J.J., 78352 Jouy-en-Josas Cedex,
France
Received 17 February 2000/Accepted 5 May 2000
In contrast to the vast majority of cellular proteins, rotavirus
proteins are translated from capped but nonpolyadenylated mRNAs. The viral nonstructural protein NSP3 specifically
binds the 3'-end consensus sequence of viral mRNAs and
interacts with the eukaryotic translation initiation factor eIF4G. Here
we show that expression of NSP3 in mammalian cells allows the efficient translation of virus-like mRNA. A synergistic effect between
the cap structure and the 3' end of rotavirus mRNA was
observed in NSP3-expressing cells. The enhancement of viral
mRNA translation by NSP3 was also observed in a rabbit
reticulocyte lysate translation system supplemented with recombinant
NSP3. The use of NSP3 mutants indicates that its RNA- and eIF4G-binding
domains are both required to enhance the translation of viral
mRNA. The results reported here show that NSP3 forms a link
between viral mRNA and the cellular translation machinery and
hence is a functional analogue of cellular poly(A)-binding protein.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Efficient Translation of Rotavirus mRNA Requires Simultaneous
Interaction of NSP3 with the Eukaryotic Translation Initiation
Factor eIF4G and the mRNA 3' End


*
Corresponding author. Mailing address: Laboratoire de
Virologie et Immunologie Moléculaires INRA, C.R.J.J., Domaine de
Vilvert, 78352 Jouy-en-Josas Cedex, France. Phone: 33-(0)1 34 65 26 11. Fax: 33-(0)1 34 65 26 21. E-mail:
poncet{at}biotec.jouy.inra.fr.
Present address: Laboratory of Infectious Diseases, National
Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.
Present address: Medicina Interna-Hepatologia, Hospitals Generals
Vall d'Hebron, 08035 Barcelona, Spain.
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