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Journal of Virology, April 2006, p. 3844-3852, Vol. 80, No. 8
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.8.3844-3852.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of Functional Domains of Equine Infectious Anemia Virus Rev Suggests a Bipartite RNA-Binding Domain

Jae-Hyung Lee,1,2,{dagger} Sean C. Murphy,3,{dagger},{ddagger} Michael Belshan,3,§ Wendy O. Sparks,3 Yvonne Wannemuehler,3 Sijun Liu,3 Thomas J. Hope,4 Drena Dobbs,1,2 and Susan Carpenter1,3*

Bioinformatics and Computational Biology Program,1 Department of Genetics, Development and Cell Biology,2 Department of Veterinary Microbiology and Preventive Medicine, Iowa State University, Ames, Iowa 50011,3 Department of Cell and Molecular Biology, Northwestern University, Chicago, Illinois 606114

Received 21 July 2005/ Accepted 16 January 2006

Equine infectious anemia virus (EIAV) Rev is an essential regulatory protein that facilitates expression of viral mRNAs encoding structural proteins and genomic RNA and regulates alternative splicing of the bicistronic tat/rev mRNA. EIAV Rev is characterized by a high rate of genetic variation in vivo, and changes in Rev genotype and phenotype have been shown to coincide with changes in clinical disease. To better understand how genetic variation alters Rev phenotype, we undertook deletion and mutational analyses to map functional domains and to identify specific motifs that are essential for EIAV Rev activity. All functional domains are contained within the second exon of EIAV Rev. The overall organization of domains within Rev exon 2 includes a nuclear export signal, a large central region required for RNA binding, a nonessential region, and a C-terminal region required for both nuclear localization and RNA binding. Subcellular localization of green fluorescent protein-Rev mutants indicated that basic residues within the KRRRK motif in the C-terminal region of Rev are necessary for targeting of Rev to the nucleus. Two separate regions of Rev were necessary for RNA binding: a central region encompassing residues 57 to 130 and a C-terminal region spanning residues 144 to 165. Within these regions were two distinct, short arginine-rich motifs essential for RNA binding, including an RRDRW motif in the central region and the KRRRK motif near the C terminus. These findings suggest that EIAV Rev utilizes a bipartite RNA-binding domain.

* Corresponding author. Present address: Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164-7040. Phone: (509) 335-6043. Fax: (509) 335-8529. E-mail: scarp{at}vetmed.wsu.edu.

{dagger} J.H.L. and S.C.M. contributed equally to this work.

{ddagger} Present address: Department of Pathology, Northwestern University, Chicago, IL 60611.

§ Present address: Department of Medical Microbiology and Immunology, Creighton University, Omaha, NE 68178.

Journal of Virology, April 2006, p. 3844-3852, Vol. 80, No. 8
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.8.3844-3852.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Groom, H. C. T., Anderson, E. C., Lever, A. M. L. (2009). Rev: beyond nuclear export. J. Gen. Virol. 90: 1303-1318 [Abstract] [Full Text]  
  • Bogerd, H. P., Tallmadge, R. L., Oaks, J. L., Carpenter, S., Cullen, B. R. (2008). Equine Infectious Anemia Virus Resists the Antiretroviral Activity of Equine APOBEC3 Proteins through a Packaging-Independent Mechanism. J. Virol. 82: 11889-11901 [Abstract] [Full Text]  
  • Sparks, W. O., Dorman, K. S., Liu, S., Carpenter, S. (2008). Naturally arising point mutations in non-essential domains of equine infectious anemia virus Rev alter Rev-dependent nuclear-export activity. J. Gen. Virol. 89: 1043-1048 [Abstract] [Full Text]  


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