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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.

Original publication




Journal article



Publication Date





59 - 67


Amino Acid Sequence, Antibodies, Monoclonal, Antibodies, Viral, Base Sequence, Endoribonucleases, Epitopes, Models, Biological, Molecular Sequence Data, RNA, Viral, Retroelements, Retroviridae, Viral Proteins, Virion