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Journal of virology1994; 68(3); 1998-2001; doi: 10.1128/JVI.68.3.1998-2001.1994

Posttranscriptional effector domains in the Rev proteins of feline immunodeficiency virus and equine infectious anemia virus.

Abstract: By systematically dissecting the Rev proteins of feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV), we have identified within each a short peptide that is functionally interchangeable with the effector domains found in Rev-like proteins from other retroviruses. The active sequences from FIV and EIAV differ in several respects from other known effectors and may represent a distinct class of effector domain.
Publication Date: 1994-03-01 PubMed ID: 8107262PubMed Central: PMC236666DOI: 10.1128/JVI.68.3.1998-2001.1994Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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The research article focuses on the identification and analysis of a specific region within the Rev proteins of both feline immunodeficiency virus (FIV) and equine infectious anemia virus (EIAV) that they discovered to be interchangeable with effector domains in other retroviruses; they suggest these sequences may represent a new class of effector domain.

Rev Proteins and Effector Domains

  • The researchers were primarily focusing on Rev proteins, which are crucial components in the replication cycle of retroviruses, including FIV and EIAV.
  • The Rev proteins support the transportation of viral RNA from the nucleus to the cytoplasm in the host cells, facilitating the assembly of new virus particles.
  • Specifically, the researchers were interested in the ‘effector domains’ of the Rev proteins. These domains are responsible for their activity, that is, they play a key role in enabling the communication and interaction between the protein and other molecules within the cell.

Identification and Analysis of New Effector Domains

  • Through systematic analysis and dissection of the Rev proteins found in FIV and EIAV, researchers identified a short peptide, a small portion of the protein, that appears to function the same way as effector domains in other retroviruses.
  • This observation led them to suggest that this specific region of the Rev proteins might be interchangeable with the effector domains found in other members of the retrovirus family.

Potential New Classification of Effector Domains

  • The researchers found that the identified sequence in Rev proteins from FIV and EIAV showed differences when compared to other known effector domains.
  • These differences in the newly discovered sequences led them to suggest that these particular sequences could represent a different class of effector domain.
  • The differences could mean the functional attributes of these effector domains are somehow unique, and sheds light on the complexity and diversity of the mechanisms employed by different viruses within the retrovirus family.

Cite This Article

APA
Mancuso VA, Hope TJ, Zhu L, Derse D, Phillips T, Parslow TG. (1994). Posttranscriptional effector domains in the Rev proteins of feline immunodeficiency virus and equine infectious anemia virus. J Virol, 68(3), 1998-2001. https://doi.org/10.1128/JVI.68.3.1998-2001.1994

Publication

ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 68
Issue: 3
Pages: 1998-2001

Researcher Affiliations

Mancuso, V A
  • Department of Pathology, University of California, San Francisco 94143-0506.
Hope, T J
    Zhu, L
      Derse, D
        Phillips, T
          Parslow, T G

            MeSH Terms

            • Amino Acid Sequence
            • DNA Mutational Analysis
            • Gene Products, rev / genetics
            • Gene Products, rev / pharmacology
            • Immunodeficiency Virus, Feline / genetics
            • Infectious Anemia Virus, Equine / genetics
            • Molecular Sequence Data
            • RNA Processing, Post-Transcriptional / drug effects
            • Recombinant Proteins / pharmacology
            • Sequence Homology, Amino Acid
            • Structure-Activity Relationship

            Grant Funding

            • AI29313 / NIAID NIH HHS
            • GM43574 / NIGMS NIH HHS

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            Citations

            This article has been cited 31 times.