The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virus.
The interaction between the infectious bursal disease virus (IBDV) capsid proteins VP2 and VP3 has been analyzed in vivo using baculovirus expression vectors. Data presented here demonstrate that the 71-amino acid C-terminal-specific domain of pVP2, the VP2 precursor, is essential for the establishment of the VP2-VP3 interaction. Additionally, we show that coexpression of the pVP2 and VP3 polypeptides from independent genes results in the assembly of virus-like particles (VLPs). This observation demonstrates that these two polypeptides contain the minimal information required for capsid assembly, and that this process does not require the presence of the precursor polyprotein.
Oña
Ana
A
Department of Biología Molecular y Celular, Centro Nacional de Biotecnología, Cantoblanco, 28049 Madrid, Spain.
Luque
Daniel
D
Abaitua
Fernando
F
Maraver
Antonio
A
Castón
José R
JR
Rodríguez
Jose F
JF
D016367:Baculoviridae / Q000235:genetics; D005822:Genetic Vectors; D007243:Infectious bursal disease virus / Q000235:genetics / Q000378:metabolism*; D016366:Open Reading Frames; D011498:Protein Precursors / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D015678:Viral Structural Proteins / Q000235:genetics / Q000378:metabolism*; D019065:Virus Assembly
D011498:Protein Precursors; C082513:VP2 protein, infectious bursal disease virus; C478244:VP3 protein, infectious bursal disease virus; D015678:Viral Structural Proteins