Nucleic Acids Research Advance Access originally published online on February 7, 2007
Nucleic Acids Research 2007 35(5):1522-1532; doi:10.1093/nar/gkl1127
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Nucleic Acids Research, 2007, Vol. 35, No. 5 1522-1532
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Rabies virus matrix protein interplay with eIF3, new insights into rabies virus pathogenesis
1Unité de la Régulation de la Traduction Eucaryote et Virale, CNRS URA 1966, 2Unité de Génétique Papillomavirus et Cancer Humain, 3Plate-forme de Biophysique des Macromolecules et de leurs interactions, 4Unité Postulante des Stratégies Antivirales, Institute Pasteur, 75015 Paris, France and 5Department of Biochemistry and Molecular Medicine. School of Medicine. University of California Davis, Davis, CA 95616, USA
*To whom the correspondence should be addressed. Tel: 01 45 68 87 53; Fax: 01 45 68 89 66; Email: yjacob{at}pasteur.fr Correspondence may also be addressed to Katherine M. Kean; E-mail: kathiemb{at}pasteur.fr
Received September 27, 2006. Revised December 8, 2006. Accepted December 11, 2006.
Viral proteins are frequently multifunctional to accommodate the high density of information encoded in viral genomes. Matrix (M) protein of negative-stranded RNA viruses such as Rhabdoviridae is one such example. Its primary function is virus assembly/budding but it is also involved in the switch from viral transcription to replication and the concomitant down regulation of host gene expression. In this study we undertook a search for potential rabies virus (RV) M protein's cellular partners. In a yeast two-hybrid screen the eIF3h subunit was identified as an M-interacting cellular factor, and the interaction was validated by co-immunoprecipitation and surface plasmon resonance assays. Upon expression in mammalian cell cultures, RV M protein was localized in early small ribosomal subunit fractions. Further, M protein added in trans inhibited in vitro translation on mRNA encompassing classical (Kozak-like) 5'-UTRs. Interestingly, translation of hepatitis C virus IRES-containing mRNA, which recruits eIF3 via a different noncanonical mechanism, was unaffected. Together, the data suggest that, as a complement to its functions in virus assembly/budding and regulation of viral transcription, RV M protein plays a role in inhibiting translation in virus-infected cells through a protein–protein interaction with the cellular translation machinery.
Two authors contributed equally to this work Present address: Eléonore Real, CSHL, New York, NY 11724. Andrew M. Borman, Mycology Reference Laboratory, Health Protection Agency, Bristol, UK. Anastassia V. Komarova, Unité INSERM 716, IGM, rue Juliette Dodu, 75010 Paris, France.
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