This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Beisel, C E Articles by Rice, N R Search for Related Content PubMed PubMed Citation Articles by Beisel, C E Articles by Rice, N R

 Previous Article  |  Next Article 

J Virol. 1993 February; 67(2): 832-842

Analysis of multiple mRNAs from pathogenic equine infectious anemia virus (EIAV) in an acutely infected horse reveals a novel protein, Ttm, derived from the carboxy terminus of the EIAV transmembrane protein.

Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research and Development Center, Maryland 21702.

ABSTRACT

Transcription of pathogenic equine infectious anemia virus (EIAV) in an acutely infected horse was examined by using the polymerase chain reaction and nucleotide sequencing. Four spliced transcripts were identified in liver tissue, in contrast to the multiplicity of alternatively spliced messages reported for in vitro-propagated human immunodeficiency virus, simian immunodeficiency virus, and, to a lesser extent, EIAV. Nucleotide sequence analysis demonstrated that three of these mRNAs encode known viral proteins: the envelope precursor, the product of the S2 open reading frame, and the regulatory proteins Tat and Rev. The fourth transcript encodes a novel Tat-TM fusion protein, Ttm. Ttm is a 27-kDa protein translated from the putative tat CTG initiation codon and containing the carboxy-terminal portion of TM immediately downstream from the membrane-spanning domain. p27ttm is expressed in EIAV-infected canine cells and was recognized by peptide antisera against both Tat and TM. Cells transfected with ttm cDNA also expressed p27ttm, which appeared to be localized to the endoplasmic reticulum or Golgi apparatus by indirect immunofluorescence. The carboxy terminus of lentiviral TM proteins has previously been shown to influence viral infectivity, growth kinetics, and cytopathology, suggesting that Ttm plays an important role in the EIAV life cycle.

This article has been cited by other articles:

• Lee, J.-H., Murphy, S. C., Belshan, M., Sparks, W. O., Wannemuehler, Y., Liu, S., Hope, T. J., Dobbs, D., Carpenter, S. (2006). Characterization of Functional Domains of Equine Infectious Anemia Virus Rev Suggests a Bipartite RNA-Binding Domain.. J. Virol. 80: 3844-3852 [Abstract] [Full Text]  
• Mertz, J. A., Simper, M. S., Lozano, M. M., Payne, S. M., Dudley, J. P. (2005). Mouse Mammary Tumor Virus Encodes a Self-Regulatory RNA Export Protein and Is a Complex Retrovirus. J. Virol. 79: 14737-14747 [Abstract] [Full Text]  
• Belshan, M., Park, G. S., Bilodeau, P., Stoltzfus, C. M., Carpenter, S. (2000). Binding of Equine Infectious Anemia Virus Rev to an Exon Splicing Enhancer Mediates Alternative Splicing and Nuclear Export of Viral mRNAs. Mol. Cell. Biol. 20: 3550-3557 [Abstract] [Full Text]  
• Oaks, J. L., McGuire, T. C., Ulibarri, C., Crawford, T. B. (1998). Equine Infectious Anemia Virus Is Found in Tissue Macrophages during Subclinical Infection. J. Virol. 72: 7263-7269 [Abstract] [Full Text]  
• Harris, M. E., Gontarek, R. R., Derse, D., Hope, T. J. (1998). Differential Requirements for Alternative Splicing and Nuclear Export Functions of Equine Infectious Anemia Virus Rev Protein. Mol. Cell. Biol. 18: 3889-3899 [Abstract] [Full Text]  
• Latimer, M., Ernst, M. K., Dunn, L. L., Drutskaya, M., Rice, N. R. (1998). The N-Terminal Domain of Ikappa Balpha Masks the Nuclear Localization Signal(s) of p50 and c-Rel Homodimers. Mol. Cell. Biol. 18: 2640-2649 [Abstract] [Full Text]