An Immunological Analysis of Ty1 Virus-like Particle Structure

• Published in: Virology (New York, N.Y.) Vol. 207; no. 1; pp. 59 - 67
• Main Authors: Brookman, Jayne L., Stott, Andrew J., Cheeseman, Philip J., Burns, Nigel R., Adams, Sally E., Kingsman, Alan J., Gull, K.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 20.02.1995
• Subjects: Amino Acid Sequence; Antibodies, Monoclonal; Antibodies, Viral; Base Sequence; Endoribonucleases; Epitopes - analysis; Models, Biological; Molecular Sequence Data; Retroelements - immunology; Retroelements - physiology; Retroviridae - immunology; Retroviridae - physiology; Retroviridae - ultrastructure; RNA, Viral - metabolism; Viral Proteins - analysis; Viral Proteins - immunology; Virion - immunology; Virion - ultrastructure
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1995.1051

We present an immunological characterization of the Ty1 virus-like particle (VLP). A panel of monoclonal and polyclonal antibodies were raised against the TYA particle-forming protein. Using these antibodies in epitope availability assays two N-terminal regions of the TYA protein were mapped projecting from or at the surface of the proteinaceous shell of the VLP. Two different C-termini of the TYA protein, corresponding to the C-terminus of the full-length and truncated forms, were seen to be buried within the particle core and not available for antibody binding. RNase accessibility studies demonstrated a difference in the porosity of the protein shell surrounding the Ty1 nucleic acid between different particle types, suggesting differences in subunit organization.