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Reactivity with polyclonal and monoclonal antibodies suggested that neutralizing epitopes were functionally unaltered on the expressed VP4.

Moreover, two amino acid substitutions observed in the VP4 gene were conserved between two or more strain pairs.

WIN 52035-2 was found to inhibit the first step of uncoating, release of VP4.

The membrane permeability induced by recombinant VP4 was influenced by pH and was comparable to permeability induced by infectious virions.

The outer capsid proteins VP4 and VP7 are highly variable and represent the major neutralizing antigens.

VP22 is believed to have certain functions in viral infection apart from virus assembly.

Separate epitopes in VP22 were defined for T-cell clones from each of three patients.

These results indicate that fusion of VP22 to an antigen gene may greatly enhance the potency of RNA replicon vaccines.

Finally, the transcriptional inhibitory effect of VP22 on other viral promoters was demonstrated by the analysis of beta-galactosidase activities in internal controls.

VP22 fusion may enhance the efficiency of non-viral gene delivery when combined with the appropriate therapeutic transgene, target tissue and transfection method.

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