AN IMMUNOLOGICAL ANALYSIS OF TY1 VIRUS-LIKE PARTICLE STRUCTURE

We present an immunological characterization of the Ty1 virus-like par ticle (VLP). A panel of monoclonal and polyclonal antibodies were rais ed 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 sh ell of the VLP. Two different C-termini of the TYA protein, correspond ing to the C-terminus of the full-length and truncated forms, were see n 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 betwee n different particle types, suggesting differences in subunit organiza tion. (C) 1995 Academic Press, Inc.