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Biochemical and biophysical research communications2004; 324(3); 1108-1115; doi: 10.1016/j.bbrc.2004.09.154

Equine papillomavirus type 1: complete nucleotide sequence and characterization of recombinant virus-like particles composed of the EcPV-1 L1 major capsid protein.

Abstract: Equus caballus papillomavirus type 1 (EcPV-1) was isolated from a cutaneous papilloma, the most common neoplasm in horses. The complete EcPV-1 nucleotide sequence and genomic organization were determined. Phylogenetic analysis showed that EcPV-1 is a close-to-root papillomavirus, with only distant relationships to the fibropapillomaviruses and the benign cutaneous papillomaviruses. To produce EcPV-1 virus-like particles (VLPs), the EcPV-1 L1 major capsid protein was expressed in insect cells using a recombinant baculovirus vector. The self-assembled EcPV-1 VLPs were morphologically indistinguishable from wild type papillomavirus virions. Monoclonal antibodies were developed against intact and denatured EcPV-1 VLPs. When tested by ELISA, all monoclonal antibodies produced against intact (#18) and some against denatured EcPV-1 VLPs (#16) reacted with intact EcPV-1 VLPs only, demonstrating that the VLPs carry type-specific conformational as well as linear epitopes on their surface. Recombinant EcPV-1 VLPs offer the potential of a noninfectious vaccine to prevent and eradicate equine cutaneous papillomatosis.
Publication Date: 2004-10-16 PubMed ID: 15485669DOI: 10.1016/j.bbrc.2004.09.154Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research article discusses the detailed examination and sequencing of Equus caballus papillomavirus type 1 (EcPV-1), a type of equine papillomavirus. The study also evaluates the potential of virus-like particles (VLPs) composed of EcPV-1’s major capsid protein to act as a noninfectious vaccine candidate for equine cutaneous papillomatosis.

Sequencing and Analysis of EcPV-1

  • The isolation of EcPV-1 was carried out from a horse’s cutaneous papilloma, which is a common type of tumor observed in horses.
  • Through analyzing the complete nucleotide sequence and genomic structure of the virus, the researchers were able to establish its phylogenetic position. In evolution terms, EcPV-1 is a fundamental papillomavirus type having distant relationships to fibropapillomaviruses and benign cutaneous papillomaviruses.

Production of EcPV-1 Virus-Like Particles (VLPs)

  • For the production of VLPs, the researchers employed a technique involving the expression of EcPV-1’s L1 major capsid protein in insect cells via a baculovirus vector. This vector encourages the cells to produce the protein.
  • The resultant VLPs were structurally identical to wild type papillomavirus virions, demonstrating their capacity to self-assemble into functional virus-like structures in vitro.

Monoclonal Antibodies and VLPs

  • Monoclonal antibodies, produced specifically against these EcPV-1 VLPs, were also studied. These antibodies were developed against both intact and denatured VLPs.
  • ELISA testing confirmed that these antibodies were successful in identifying intact EcPV-1 VLPs, suggesting they contains type-specific conformational and linear epitopes or specific binding sites on their surface, crucial for immune response.

Potential for Vaccine Development

  • Given that the produced VLPs were equivalent to the wild type virus, and that the developed antibodies were successful in identifying these, the study concludes with the potential of these VLPs to be used as noninfectious vaccines.
  • If further validated and developed, such a vaccine could effectively prevent or eradicate equine cutaneous papillomatosis in horses, having a significant impact on equine health.

Cite This Article

APA
Ghim SJ, Rector A, Delius H, Sundberg JP, Jenson AB, Van Ranst M. (2004). Equine papillomavirus type 1: complete nucleotide sequence and characterization of recombinant virus-like particles composed of the EcPV-1 L1 major capsid protein. Biochem Biophys Res Commun, 324(3), 1108-1115. https://doi.org/10.1016/j.bbrc.2004.09.154

Publication

ISSN: 0006-291X
NlmUniqueID: 0372516
Country: United States
Language: English
Volume: 324
Issue: 3
Pages: 1108-1115

Researcher Affiliations

Ghim, Shin-Je
  • Laboratory of Vaccinology, John Graham Brown Cancer Center, University of Louisville Health Science Center, Louisville, KY, USA.
Rector, Annabel
    Delius, Hajo
      Sundberg, John P
        Jenson, A Bennett
          Van Ranst, Marc

            MeSH Terms

            • Amino Acid Motifs
            • Animals
            • Antibodies, Monoclonal / chemistry
            • Baculoviridae / metabolism
            • Capsid Proteins / chemistry
            • Capsid Proteins / genetics
            • Cell Line
            • DNA / chemistry
            • Electrophoresis, Polyacrylamide Gel
            • Enzyme-Linked Immunosorbent Assay
            • Epitopes / chemistry
            • Genome, Viral
            • Horses
            • Immunoblotting
            • Insecta
            • Mice
            • Mice, Inbred BALB C
            • Oncogene Proteins, Viral / chemistry
            • Open Reading Frames
            • Papillomaviridae / genetics
            • Phylogeny
            • Protein Conformation
            • Recombinant Proteins / chemistry
            • Recombination, Genetic
            • Sequence Analysis, DNA
            • Virion

            Citations

            This article has been cited 12 times.
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