Rabies virus matrix protein interplay with elF3, new insights into rabies virus pathogenesis

Komarova, A. V., Rea, E., Borman, A. M., Brocard, M., England, P., Tordo, N., Hershey, J. W. B., Kean, K. M., Jacob, Y. (March 2007) Rabies virus matrix protein interplay with elF3, new insights into rabies virus pathogenesis. Nucleic Acids Research, 35 (5). pp. 1522-1532. ISSN 03051048 (ISSN)

[thumbnail of Paper]
Preview
PDF (Paper)
Rabies virus matrix protein.pdf - Published Version

Download (4MB) | Preview
URL: http://www.ncbi.nlm.nih.gov/pubmed/17287294
DOI: 10.1093/nar/gkl1127

Abstract

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 elF3h 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 elF3 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 proteinprotein interaction with the cellular translation machinery.

Item Type: Paper
Uncontrolled Keywords: VESICULAR STOMATITIS-VIRUS TRANSLATION INITIATION COMPLEX BINDING-PROTEIN EUKARYOTIC INITIATION-FACTOR-3 CAP-POLY(A) SYNERGY MESSENGER-RNAS GLYCOPROTEIN G ENTRY SITES HEPATITIS-C UBIQUITIN
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > matrix protein
organism description > virus > rabies virus
organism description > yeast
CSHL Authors:
Communities: CSHL Post Doctoral Fellows
CSHL labs > Malinow lab
Depositing User: CSHL Librarian
Date: March 2007
Date Deposited: 11 Nov 2011 19:05
Last Modified: 02 May 2013 16:52
PMCID: PMC1865048
Related URLs:
URI: https://repository.cshl.edu/id/eprint/23069

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving