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Journal of virology1993; 67(12); 7317-7323; doi: 10.1128/JVI.67.12.7317-7323.1993

Identification of the activation domain of equine infectious anemia virus rev.

Abstract: Several members of the lentivirus family of complex retroviruses have been shown to encode proteins that are functionally equivalent to the Rev posttranscriptional regulatory protein of human immunodeficiency virus type 1 (HIV-1). Furthermore, the domain organization of HIV-1 Rev, featuring a highly basic N-terminal RNA binding domain and a leucin-rich C-terminal effector domain, has also been shown to be highly conserved among Rev proteins derived from not only the primate but also the ovine and caprine lentiviruses. Although it has therefore appeared highly probable that the lentivirus equine infectious anemia virus (EIAV) also encodes a Rev, the predicted amino acid sequence of this putative EIAV regulatory protein does not display any evident homology to the basic and leucine-rich motifs characteristic of other known Rev proteins. By fusion of different segments of the proposed EIAV Rev protein to the well-defined RNA binding domain of either HIV-1 or visna virus Rev, we have identified a segment of this EIAV protein that can efficiently substitute in cis for the otherwise essential activation motif. Interestingly, the minimal EIAV Rev activation motif identified in this study comprises approximately 18 amino acids located toward the protein N terminus that lack any evident similarity to the leucine-rich activation domains found in these other lentivirus Rev proteins. It therefore appears that the Rev protein of EIAV, while analogous in function to Rev proteins defined in lentiviruses of primate, ovine, and caprine origin, is nevertheless distinguished by an entirely novel domain organization.
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Publication Date: 1993-12-01 PubMed ID: 8230455PubMed Central: PMC238195DOI: 10.1128/JVI.67.12.7317-7323.1993Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigates the activation domain of a regulatory protein, Rev, in the lentivirus equine infectious anemia virus (EIAV). This protein is found to have a unique structure that differs from other Rev proteins in the lentivirus family.

Introduction of the Research

  • The article studies the Rev posttranscriptional regulatory protein found in the lentivirus family of complex retroviruses. This protein has been identified in other members of the lentivirus family, including the human immunodeficiency virus type 1 (HIV-1).
  • Although the domain structure of Rev, characterized by an N-terminal RNA binding domain, and a leucin-rich C-terminal effector domain, is conserved across primate, ovine, and caprine lentiviruses, it is suggested that there’s a difference in the structure of Rev in EIAV.

Study of EIAV’s Rev Protein

  • The researchers examined EIAV’s Rev protein as the predicted amino acid sequence of this protein doesn’t display evident homology to the leucine-rich and basic motifs that are characteristic of other known Rev proteins.
  • To understand the structure of EIAV’s Rev, researchers fused different segments of this protein to the well-defined RNA binding domain of either HIV-1 or visna virus Rev.
  • Through this, they identified a segment of the EIAV protein that can efficiently function as the activation motif, a key component of the Rev protein.

Findings About EIAV’s Rev

  • The researchers found that the minimal activation motif of EIAV’s Rev contains about 18 amino acids that are located toward the protein’s N terminus.
  • Interestingly, this motif doesn’t display evident similarity to the leucine-rich activation domains typically found in other lentivirus Rev proteins.
  • This suggests that, while the function of EIAV’s Rev mirrors that of Rev proteins from lentiviruses of primate, ovine, and caprine origin, its domain organization is entirely novel.

Cite This Article

APA
Fridell RA, Partin KM, Carpenter S, Cullen BR. (1993). Identification of the activation domain of equine infectious anemia virus rev. J Virol, 67(12), 7317-7323. https://doi.org/10.1128/JVI.67.12.7317-7323.1993

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 67
Issue: 12
Pages: 7317-7323

Researcher Affiliations

Fridell, R A
  • Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710.
Partin, K M
    Carpenter, S
      Cullen, B R

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Cell Line
        • Cloning, Molecular
        • Gene Expression Regulation, Viral
        • Genes, rev
        • HIV-1 / genetics
        • Infectious Anemia Virus, Equine / genetics
        • Molecular Sequence Data
        • Open Reading Frames / genetics
        • Recombinant Fusion Proteins
        • Regulatory Sequences, Nucleic Acid
        • Visna-maedi virus / genetics

        Grant Funding

        • AI-28233 / NIAID NIH HHS
        • AI-30025 / NIAID NIH HHS

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        This article has been cited 36 times.
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