VP22 is believed to have certain functions in viral infection apart from virus assembly.
2
Separate epitopes in VP22 were defined for T-cell clones from each of three patients.
3
These results indicate that fusion of VP22 to an antigen gene may greatly enhance the potency of RNA replicon vaccines.
4
Finally, the transcriptional inhibitory effect of VP22 on other viral promoters was demonstrated by the analysis of beta-galactosidase activities in internal controls.
5
VP22 fusion may enhance the efficiency of non-viral gene delivery when combined with the appropriate therapeutic transgene, target tissue and transfection method.
1
Reactivity with polyclonal and monoclonal antibodies suggested that neutralizing epitopes were functionally unaltered on the expressed VP4.
2
Moreover, two amino acid substitutions observed in the VP4 gene were conserved between two or more strain pairs.
3
WIN 52035-2 was found to inhibit the first step of uncoating, release of VP4.
4
The membrane permeability induced by recombinant VP4 was influenced by pH and was comparable to permeability induced by infectious virions.
5
The outer capsid proteins VP4 and VP7 are highly variable and represent the major neutralizing antigens.