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Home / Equine Research Bank / J Virol / Characterization of an equine herpesvirus type 1 gene encodi...
Journal of virology1988; 62(8); 2850-2858; doi: 10.1128/JVI.62.8.2850-2858.1988

Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C.

Abstract: The molecular structure of the equine herpesvirus type 1 (EHV-1) gene encoding glycoprotein 13 (gp13) was analyzed. The gene is contained within a 1.8-kilobase AccI-EcoRI restriction fragment mapping at map coordinates 0.136 to 0.148 in the UL region of the EHV-1 genome and is transcribed from right to left. Determination of the nucleotide sequence of the DNA fragment revealed a complete transcriptional unit composed of typical regulatory promoter elements upstream to a long open reading frame (1,404 base pairs) that encoded a 468-amino-acid primary translation product of 51 kilodaltons. The predicted protein has the characteristic features of a membrane-spanning protein: an N-terminal signal sequence, a hydrophobic membrane anchor region, a charged C-terminal cytoplasmic tail, and an exterior domain with nine potential N-glycosylation sites. The EHV-1 DNA sequences expressed in lambda gt11 as gp13 epitopes were present in the open reading frame. Amino acid sequences composing a major antigenic site, recognized by 35% of a panel of 42 anti-gp13 monoclonal antibodies, were identified in the N-terminal surface domain of the deduced gp13 molecule. Comparison of the EHV-1 gp13 DNA sequence with that encoding glycoproteins of other alphaherpesviruses revealed no detectable homology. However, a search for homology at the amino acid level showed regions of significant sequence similarity between the amino acids of the carboxy half of EHV-1 gp13 and those of the same region of gC-like glycoproteins of herpes simplex virus (gC-1 and gC-2), pseudorabies herpesvirus (gIII), and varicella-zoster virus (gp66). The sequences of the N-terminal portion of gp13, by contrast, were much less conserved. The results of these studies indicate that EHV-1 gp13 is the structural homolog of herpes simplex virus glycoprotein C and further suggest that the epitope-containing N-terminal amino acid sequences of the herpesvirus gC-like glycoproteins have undergone more extensive evolutionary divergence than the C-terminal sequences.
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Publication Date: 1988-08-01 PubMed ID: 2455821PubMed Central: PMC253721DOI: 10.1128/JVI.62.8.2850-2858.1988Google Scholar: Lookup
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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.

The researchers have analyzed the molecular structure of a gene in equine herpesvirus type 1 (EHV-1) that encodes a protein, glycoprotein 13 (gp13). They found that this protein shares some similarities with a glycoprotein in herpes simplex virus, suggesting shared evolutionary origins and possibly similar functions.

Molecular Structure of EHV-1 gp13 Gene

  • The gp13 gene is found within a 1.8-kilobase fragment of the EHV-1 genome, located at map coordinates 0.136 to 0.148 in the UL (unique long) region.
  • The gene is transcribed from right to left, into an open reading frame (a sequence that can potentially be translated into a protein) consisting of 1,404 base pairs.

Nucleotide Sequence, Protein Production and Membrane-Spanning Properties

  • The gene’s nucleotide sequence was revealed to include all the parts needed for gene expression: it has regulatory promoter elements (sequences of DNA that initiate transcription of a gene) that precede a long open reading frame encoding a protein.
  • The protein produced is made up of 468 amino acids and weighs 51 kilodaltons (a unit of molecular mass).
  • It was predicted that gp13 is a membrane-spanning protein based on certain characteristics: it has an N-terminal signal sequence (a sequence at the beginning of the protein that signals it to be transported to the membrane), a hydrophic membrane anchor region, a charged C-terminal cytoplasmic tail, and an exterior domain with nine potential N-glycosylation sites (sites where sugar molecules can attach – this process is important for proper protein folding and function).

Antigenic Sites and Homology to Other Viruses

  • The researchers found that 35% of a panel of 42 anti-gp13 monoclonal antibodies (laboratory-produced molecules engineered to attach to specific defects in cancer cells) recognized a major antigenic site (part of the protein that the immune system recognizes) in the N-terminal surface domain.
  • The EHV-1 gp13 DNA sequence was compared to that of glycoproteins in other members of the alphaherpesvirus family, however no detectable homology, or shared evolutionary origins, was found at the DNA level.
  • Despite the lack of DNA homology, the researchers were able to find some homology at the amino acid level in the C-terminal region of gp13 when compared to herpes simplex virus glycoproteins.
  • The researchers conclude that EHV-1 gp13 is likely a structural homolog of herpes simplex virus glycoprotein C, but the N-terminal sequences of these proteins, which contain the epitopes recognized by the immune system, have evolved more extensively.

Cite This Article

APA
Allen GP, Coogle LD. (1988). Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C. J Virol, 62(8), 2850-2858. https://doi.org/10.1128/JVI.62.8.2850-2858.1988

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 62
Issue: 8
Pages: 2850-2858

Researcher Affiliations

Allen, G P
  • Department of Veterinary Science, University of Kentucky, Lexington 40546-0099.
Coogle, L D

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Antigens, Viral / genetics
    • Base Sequence
    • Codon
    • DNA, Viral / genetics
    • Epitopes
    • Genes, Viral
    • Herpesviridae / genetics
    • Horses / microbiology
    • Molecular Sequence Data
    • Protein Conformation
    • Solubility
    • Viral Envelope Proteins / genetics

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