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Home / Equine Research Bank / J Virol / Characterization of the myristylated polypeptide encoded by ...
Journal of virology1993; 67(7); 4122-4132; doi: 10.1128/JVI.67.7.4122-4132.1993

Characterization of the myristylated polypeptide encoded by the UL1 gene that is conserved in the genome of defective interfering particles of equine herpesvirus 1.

Abstract: Equine herpesvirus 1 (EHV-1, Kentucky A strain) preparations enriched for defective interfering particles (DIPs) can readily establish persistent infection. The UL1 gene, which is conserved in the genome of DIPs that mediate persistent infection, maps between nucleotides 1418 and 2192 (258 amino acids) from the L (long) terminus. UL1 has no homology with any known gene encoded by herpes simplex virus type 1 but has limited homology to open reading frame 2 of varicella-zoster virus and the "circ" gene of bovine herpesvirus type 1. Previous work showed that the EHV-1 UL1 gene belongs to the early kinetic class and is transcribed as a 1.2-kb polyadenylated mRNA (R. N. Harty, R. R. Yalamanchili, and D. J. O'Callaghan, Virology 183:830-833, 1991). In this report, the UL1 protein was identified and characterized as a 33-kDa polypeptide in EHV-1-infected cells by using rabbit polyclonal antiserum raised against a TrpE-UL1 fusion protein (amino acids 7 to 258 of UL1) synthesized in Escherichia coli. Results from Western blot (immunoblot), immunoprecipitation, indirect immunofluorescence, and biochemical analyses indicated that the UL1 polypeptide (i) is more abundant in cells infected with DIP-enriched virus than in cells infected with standard EHV-1, (ii) is synthesized as early as 3 h postinfection (p.i.) in infection with standard virus or in infection with DIP-enriched virus preparations and increases in abundance up to 12 h p.i., (iii) appears to be associated with the rough endoplasmic reticulum-Golgi apparatus early in infection (3 to 4 h p.i.), while a diffuse cytoplasmic pattern of fluorescence is observed late in infection (7 to 8 h p.i.), (iv) is modified by myristic acid as it contains a consensus N-terminal myristylation site and is readily labeled with [3H]myristic acid, and (v) is associated with mature EHV-1 virions.
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Publication Date: 1993-07-01 PubMed ID: 8389920PubMed Central: PMC237781DOI: 10.1128/JVI.67.7.4122-4132.1993Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • 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.

This research paper investigates the UL1 gene present in defective interfering particles (DIPs) of Equine herpesvirus 1 (EHV-1, Kentucky A strain). The researchers explored the role and characteristics of the UL1 protein, discovering it to be early-acting, prevalent in DIP-enriched EHV-1 infections, and undergoing modification by myristic acid.

Research Setup and Context

  • The study focuses on the UL1 gene found in Equine herpesvirus 1 (EHV-1) – specifically in defective interfering particles (DIPs) that can establish persistent infection.
  • This gene can be mapped between nucleotides 1418 and 2192 from the long terminus. It doesn’t share homology with any other known gene in herpes simplex virus type 1 but has limited similarities to genes in varicella-zoster virus and bovine herpesvirus type 1.
  • Previous research has shown that the EHV-1 UL1 gene is early-acting and transcribed into a 1.2-kb polyadenylated mRNA. The current study seeks to identify and profile the UL1 protein in infected cells.

UL1 Protein Identification & Characterization

  • The UL1 protein was identified in EHV-1 infected cells using antiserum raised against a TrpE-UL1 fusion protein. This fusion protein was synthesized in Escherichia coli bacteria.
  • The protein was described as a 33-kDa polypeptide.
  • Various methods including Western blot, immunoprecipitation, indirect immunofluorescence, and biochemical analyses were used for characterization.

Key Results and Observations

  • It was noted that the UL1 protein is more abundant in infections with a high concentration of DIPs than in standard EHV-1 infections.
  • The protein is synthesized early after infection (3 hours post-infection) in infections with the standard virus or DIP-enriched virus. Its amount increases up to 12 hours post-infection.
  • Initially, the UL1 protein appears to associate with rough endoplasmic reticulum-Golgi apparatus (3 to 4 hours post-infection). Later on (7 to 8 hours post-infection), it shows a diffuse cytoplasmic pattern of fluorescence.
  • The protein is modified by myristic acid and indeed contains a consensus N-terminal myristylation site. Myristylation was confirmed by successfully labeling the protein with radioactive myristic acid.
  • Lastly, the UL1 protein was found to be associated with mature EHV-1 virions, further confirming its role in infection.

Cite This Article

APA
Harty RN, Caughman GB, Holden VR, O'Callaghan DJ. (1993). Characterization of the myristylated polypeptide encoded by the UL1 gene that is conserved in the genome of defective interfering particles of equine herpesvirus 1. J Virol, 67(7), 4122-4132. https://doi.org/10.1128/JVI.67.7.4122-4132.1993

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 67
Issue: 7
Pages: 4122-4132

Researcher Affiliations

Harty, R N
  • Department of Microbiology and Immunology, Louisiana State University Medical Center, Shreveport 71130-3932.
Caughman, G B
    Holden, V R
      O'Callaghan, D J

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Cloning, Molecular
        • Consensus Sequence
        • Defective Viruses / genetics
        • Fluorescent Antibody Technique
        • Genes, Viral
        • Herpesvirus 1, Equid / genetics
        • In Vitro Techniques
        • L Cells
        • Mice
        • Molecular Sequence Data
        • Myristates
        • Sequence Alignment
        • Viral Interference
        • Viral Proteins / chemistry
        • Viral Proteins / genetics
        • Viral Proteins / immunology
        • Viral Proteins / metabolism
        • Viral Structural Proteins / genetics

        Grant Funding

        • AI 22001 / NIAID NIH HHS
        • AI 22894 / NIAID NIH HHS

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