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Virology1984; 134(1); 184-195; doi: 10.1016/0042-6822(84)90284-8

Equine cytomegalovirus: structural proteins of virions and nucleocapsids.

Abstract: Enveloped virions and nucleocapsids of equine cytomegalovirus (ECMV; equine herpesvirus type 2) have been purified from the supernatants and the nuclear extracts of infected rabbit kidney (RK) cells, respectively, and their structural protein compositions have been analyzed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that ECMV nucleocapsids were composed of nine proteins (average molecular weights = 148K, 52K, 49.5K, 46K, 43.5K, 38.5K, 27K, 20K, and 18K), which together constituted 89% of the total nucleocapsid protein on the basis of incorporated 3H-labeled amino acids. The 148K protein comprised 47.3% of the total protein and thus appeared to be similar in molecular weight and proportional composition to the major capsid proteins of other herpesviruses. Purified virions were composed of 37 proteins whose average molecular weights ranged from 14K to greater than 200K. Three intense glycoprotein bands (83K, 78K, and 73.5K) as well as four less intensely labeled glycoproteins were detected in [3H]glucosamine-labeled virion preparations. At least 14 structural proteins were readily detected in extracts of infected cells which had been [35S]methionine labeled late in infection, and 11 of these were immunoprecipitated by rabbit antiserum against purified virions. The protein composition of ECMV differs substantially from those of equine herpesvirus type 1 and type 3 as well as from those of other herpesviruses.
Publication Date: 1984-04-15 PubMed ID: 6324468DOI: 10.1016/0042-6822(84)90284-8Google 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

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The study investigates the structural protein composition of equine cytomegalovirus, revealing significant differences between it and other herpesviruses, including equine herpesvirus type 1 and 3.

Study Objective and Methodology

  • The objective of the research was to examine and understand the structural proteins of two structures of equine cytomegalovirus (ECMV, also known as equine herpesvirus type 2); the enveloped virions and nucleocapsids.
  • To analyze their protein compositions, the researchers used purified virions and nucleocapsids collected from the supernatants (liquid part left after removing solids) and nuclear extracts of infected rabbit kidney cells, respectively.
  • The structural protein compositions were then analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis, a common method for analyzing proteins in labs.

Major Findings

  • The researchers found that the nucleocapsids were composed of nine proteins with different molecular weights. These proteins constituted approximately 89% of the total nucleocapsid protein.
  • Among these proteins, the 148K protein was found to comprise 47.3% of the total protein, suggesting it has similar size and distribution as the major capsid proteins in other herpesviruses.
  • Upon examination of the purified virions, the researchers identified 37 proteins with varying molecular weights. Among these, they found three prominent glycoprotein bands alongside four more less intensely labeled glycoproteins.
  • The researchers noted that at least 14 structural proteins were present in extracts of infected cells, which had been labeled with an radioisotope during latter phases of infection. Out of these, 11 proteins were immunoprecipitated (i.e., they reacted to form a solid) by a rabbit’s antiserum against purified virions.
  • Notably, the research underscores that the protein composition of ECMV diverges considerably from those of other herpesviruses, including equine herpesvirus type 1 and 3. This unique protein structure could have implications for how the virus behaves and how it may be treated or prevented.

Cite This Article

APA
Caughman GB, Staczek J, O'Callaghan DJ. (1984). Equine cytomegalovirus: structural proteins of virions and nucleocapsids. Virology, 134(1), 184-195. https://doi.org/10.1016/0042-6822(84)90284-8

Publication

ISSN: 0042-6822
NlmUniqueID: 0110674
Country: United States
Language: English
Volume: 134
Issue: 1
Pages: 184-195

Researcher Affiliations

Caughman, G B
    Staczek, J
      O'Callaghan, D J

        MeSH Terms

        • Animals
        • Capsid / analysis
        • Capsid / isolation & purification
        • Cell Line
        • Cytomegalovirus / analysis
        • Cytomegalovirus / isolation & purification
        • Cytomegalovirus / physiology
        • Electrophoresis, Polyacrylamide Gel
        • Glycoproteins / analysis
        • Horses / microbiology
        • Molecular Weight
        • Rabbits
        • Viral Proteins / analysis
        • Viral Structural Proteins
        • Virion / analysis
        • Virion / isolation & purification

        Grant Funding

        • AI02032 / NIAID NIH HHS
        • AI19415 / NIAID NIH HHS
        • S-507-RR05386 / NCRR NIH HHS

        Citations

        This article has been cited 3 times.
        1. Robin J, Laperrière A, Berthiaume L. Identification of the glycoproteins of lymphocystis disease virus (LDV) of fish. Arch Virol 1986;87(3-4):297-305.
          doi: 10.1007/BF01315307pubmed: 3947242google scholar: lookup
        2. Meijer H, Dormans PH, van Boven CP. Studies on rat cytomegalovirus induced structural and non-structural proteins present at (immediate-)early and late times of infection. Arch Virol 1986;89(1-4):45-56.
          doi: 10.1007/BF01309878pubmed: 3013132google scholar: lookup
        3. Staczek J. Animal cytomegaloviruses. Microbiol Rev 1990 Sep;54(3):247-65.
          doi: 10.1128/mr.54.3.247-265.1990pubmed: 2170830google scholar: lookup