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

• Published in: Biochemical and biophysical research communications Vol. 324; no. 3; pp. 1108 - 1115
• Main Authors: Ghim, Shin-Je, Rector, Annabel, Delius, Hajo, Sundberg, John P., Jenson, A. Bennett, Van Ranst, Marc
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 19.11.2004
• Subjects: Amino Acid Motifs; Animals; Antibodies, Monoclonal - chemistry; Baculoviridae - metabolism; Baculovirus; Capsid Proteins - chemistry; Capsid Proteins - genetics; Cell Line; DNA - chemistry; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Epitopes - chemistry; Equine; Equine papillomavirus; Equus caballus; Genome, Viral; Horses; Immunoblotting; Insecta; Mice; Mice, Inbred BALB C; Oncogene Proteins, Viral - chemistry; Open Reading Frames; Papillomaviridae - genetics; Papillomavirus; Phylogeny; Protein Conformation; Recombinant Proteins - chemistry; Recombination, Genetic; Sequence Analysis, DNA; Virion; Virus-like particles; Papillomavirus; Equus caballus; Equine; Virus-like particles
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2004.09.154

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.