Virus-like particles of calicivirus as epitope carriers.
The VP60 of rabbit haemorrhagic disease virus (RHDV), when expressed in baculovirus, self-assembles into virus-like particles (VLP) which are antigenically and immunogenically indistinguishable from native virions. When the N-terminal 30 amino acid residues of VP60 were deleted and substituted by a well characterized six residue epitope from bluetongue virus capsid protein VP7 (Btag), the fusion protein retained its ability to self-assemble into VLPs. However, the size of these particles was only 27 nm, compared to 40 nm of VLPs derived from native VP60. The antigenicity of both VP60 and the Btag was retained as evident from ELISA and Western blot analyses. When Btag was fused at the C-terminus of VP60 without deletion, the fusion proteins formed VLPs of 40 nm in size and also retained their antigenicity, but the Btag antigenicity appeared weak at this fusion site.
Nagesha
H S
HS
CSIRO Australian Animal Health Laboratory, Geelong, Victoria, Australia.
Wang
L F
LF
Hyatt
A D
AD
D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D001483:Base Sequence; D015153:Blotting, Western; D002213:Capsid / Q000276:immunology; D036022:Capsid Proteins; D002460:Cell Line; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D017929:Hemorrhagic Disease Virus, Rabbit / Q000276:immunology*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010957:Plasmids / Q000235:genetics; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000276:immunology; D018411:Spodoptera; D015678:Viral Structural Proteins / Q000276:immunology* / Q000378:metabolism; D014771:Virion / Q000276:immunology*; D019065:Virus Assembly
D036022:Capsid Proteins; D000939:Epitopes; D011993:Recombinant Fusion Proteins; C442520:VP2 protein, Bluetongue virus; D015678:Viral Structural Proteins; C081149:viral protein 60, rabbit hemorrhagic disease virus