An immunological analysis of Ty1 virus-like particle structure.
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.
Brookman
J L
JL
School of Biological Sciences, University of Manchester, United Kingdom.
Stott
A J
AJ
Cheeseman
P J
PJ
Burns
N R
NR
Adams
S E
SE
Kingsman
A J
AJ
Gull
K
K
D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D001483:Base Sequence; D004722:Endoribonucleases; D000939:Epitopes / Q000032:analysis; D008954:Models, Biological; D008969:Molecular Sequence Data; D012367:RNA, Viral / Q000378:metabolism; D018626:Retroelements / Q000276:immunology / Q000502:physiology*; D012190:Retroviridae / Q000276:immunology* / Q000502:physiology / Q000648:ultrastructure; D014764:Viral Proteins / Q000032:analysis / Q000276:immunology; D014771:Virion / Q000276:immunology* / Q000648:ultrastructure
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D000939:Epitopes; D012367:RNA, Viral; D018626:Retroelements; D014764:Viral Proteins; D004722:Endoribonucleases