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Journal of virology1992; 66(11); 6294-6303; doi: 10.1128/JVI.66.11.6294-6303.1992

Structural proteins of equine arteritis virus.

Abstract: We have recently shown that the genome of equine arteritis virus (EAV) contains seven open reading frames (ORFs). We now present data on the structural proteins of EAV and the assignment of their respective genes. Virions are composed of a 14-kDa nucleocapsid protein (N) and three membrane proteins designated M, GS, and GL. M is an unglycosylated protein of 16 kDa, and GS and GL are N-glycosylated proteins of 25 and 30 to 42 kDa, respectively. The broad size distribution of GL results from heterogeneous N-acetyllactosamine addition since it is susceptible to digestion by endo-beta-galactosidase. Using monospecific antisera as well as an antivirion serum, and by expression of individual ORFs, the genes for the structural proteins were identified: ORF 7 codes for N, ORF 6 for M, ORF 5 for GL, and ORF 2 for GS. With the exception of GS, the proteins are about equally abundant in EAV virions, being present at a molar ratio of 3 (N):2 (M):3 (GL). The GS protein, which is expressed at a level similar to that of M in infected cells, is strikingly underrepresented in virus particles (1 to 2%). Our data justify a distinct taxonomic position for EAV, together with lactate dehydrogenase-elevating virus and simian hemorrhagic fever virus; although coronavirus- and toroviruslike in features of transcription and translation, the virion architecture of EAV is fundamentally different.
Publication Date: 1992-11-01 PubMed ID: 1328669PubMed Central: PMC240121DOI: 10.1128/JVI.66.11.6294-6303.1992Google Scholar: Lookup
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Summary

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This research article delves into the structural proteins found in the equine arteritis virus (EAV), assigning each of them to their respective genes. The study establishes that EAV possesses a unique structural complexity among viruses, and thus merits its own distinct taxonomic categorisation.

Investigating the Structure of Equine Arteritis Virus

  • The research displays the composition of the equine arteritis virus, which is a virus affecting the horses’ respiratory system. The scientists used specific tools and processes to identify the structural proteins of the virus and link them to their respective genes.
  • The virus was found to be composed of one 14-kDa nucleocapsid protein (N) and three membrane proteins designated M, GS, and GL. These proteins were identified by using monospecific antisera, an antivirion serum, as well as by expressing individual open reading frames (ORFs), which are sections of the virus’s genome that can be decoded into proteins.

Discoveries about the Structural Proteins

  • The membrane protein M is unglycosylated and weighs 16 kDa. The other two proteins, GS and GL, are N-glycosylated and weigh 25 and between 30 to 42 kDa, respectively. The wide size range of GL is due to the heterogeneous addition of N-acetyllactosamine, which makes it susceptible to digestion by endo-beta-galactosidase.
  • The structural proteins were identified to specific genes, revealing that ORF 7 codes for N, ORF 6 for M, ORF 5 for GL, and ORF 2 for GS. These proteins have roughly the same presence in EAV virions, being present at a molar ratio of 3(N):2(M):3(GL), except for GS which is significantly less prevalent in virus particles.

Taxonomic Position of EAV

  • Although EAV shares characteristics with coronavirus and torovirus in terms of transcription and translation features, its virion structure is notably distinctive. This leads to the conclusion that EAV deserves its own unique classification, along with the lactate dehydrogenase-elevating virus and the simian hemorrhagic fever virus.
  • This research has therefore significantly contributed to understanding the structural characteristics of EAV, enriching the scientific community’s knowledge of this important equine virus and its place within virus taxonomy.

Cite This Article

APA
de Vries AA, Chirnside ED, Horzinek MC, Rottier PJ. (1992). Structural proteins of equine arteritis virus. J Virol, 66(11), 6294-6303. https://doi.org/10.1128/JVI.66.11.6294-6303.1992

Publication

ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 66
Issue: 11
Pages: 6294-6303

Researcher Affiliations

de Vries, A A
  • Department of Infectious Diseases and Immunology, Veterinary Faculty, University of Utrecht, The Netherlands.
Chirnside, E D
    Horzinek, M C
      Rottier, P J

        MeSH Terms

        • Amino Acid Sequence
        • Antibodies, Viral
        • Capsid / analysis
        • Capsid / genetics
        • Chromosome Mapping
        • Cloning, Molecular
        • Equartevirus / chemistry
        • Equartevirus / genetics
        • Genes, Viral / genetics
        • Genome, Viral
        • Glycoproteins / analysis
        • Glycoproteins / genetics
        • Molecular Sequence Data
        • Open Reading Frames / genetics
        • Protein Conformation
        • Sequence Analysis, DNA
        • Viral Matrix Proteins / analysis
        • Viral Matrix Proteins / genetics
        • Viral Structural Proteins / chemistry
        • Viral Structural Proteins / genetics
        • Virion / genetics

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