Journal of virology1993; 67(2); 832-842; doi: 10.1128/JVI.67.2.832-842.1993

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.

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.
Publication Date: 1993-02-01 PubMed ID: 8419648PubMed Central: PMC237437DOI: 10.1128/JVI.67.2.832-842.1993Google Scholar: Lookup
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Summary

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The research examines the transcription of equine infectious anemia virus (EIAV) in an acutely infected horse and discovers a novel protein known as Ttm.

Methodology

  • The research involved analyzing genetic transcription of an EIAV in an infected horse. This was accomplished using polymerase chain reaction (a method used to amplify a specific segment of DNA) and nucleotide sequencing (a process of identifying the exact sequence of nucleotides in a DNA molecule).

Results

  • Research found four specific spliced transcripts in liver tissue. Spliced transcripts are results of gene regulation where portions of the pre-messenger RNA (pre-mRNA) are removed before the molecule is used to produce proteins.
  • These found transcripts contrast with the multitude of alternately spliced messages that have been reported in research on human immunodeficiency virus, simian immunodeficiency virus, and to a lesser extent, EIAV.
  • Nucleotide sequence analysis showed that three of these mRNAs produce known viral proteins: the envelope precursor, the product of the S2 open reading frame, and the regulatory proteins Tat and Rev.
  • The fourth transcript recorded codes for a novel protein fusion known as Ttm. Ttm is identified as a 27-kDa protein, translated from the theoretical tat CTG initiation codon, and features the carboxy-terminal portion of TM right after the membrane-spanning domain.

Expression and Localization of Ttm

  • The Ttm protein was found to be expressed in EIAV-infected canine cells and was identified by peptide antisera against both Tat and TM.
  • Cells transfected with ttm cDNA also expressed the Ttm protein, and it appears to be localized to the endoplasmic reticulum or Golgi apparatus according to indirect immunofluorescence.
  • The carboxy terminus of lentiviral TM proteins, like Ttm, has already been shown to influence viral infectivity, growth kinetics, and cytopathology. Therefore this suggests the novel Ttm protein likely plays a crucial role in the EIAV lifecycle.

Cite This Article

APA
Beisel CE, Edwards JF, Dunn LL, Rice NR. (1993). 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. J Virol, 67(2), 832-842. https://doi.org/10.1128/JVI.67.2.832-842.1993

Publication

ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 67
Issue: 2
Pages: 832-842

Researcher Affiliations

Beisel, C E
  • Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research and Development Center, Maryland 21702.
Edwards, J F
    Dunn, L L
      Rice, N R

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Base Sequence
        • Cell Compartmentation
        • Endoplasmic Reticulum
        • Equine Infectious Anemia / genetics
        • Exons / genetics
        • Gene Products, rev
        • Gene Products, tat
        • Golgi Apparatus
        • Horses
        • Membrane Proteins
        • Molecular Sequence Data
        • Polymerase Chain Reaction
        • RNA Splicing
        • RNA, Messenger / genetics
        • RNA, Viral / genetics
        • Sequence Homology, Nucleic Acid
        • Transcription, Genetic
        • Viral Envelope Proteins / genetics

        Grant Funding

        • N01-CO-74101 / NCI NIH HHS

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