Characterization of hepatitis A virus structural proteins.

HAV particles isolated from infected cells banded at buoyant densities of 1.42, 1.32, and 1.20 g/ml, and distinctive protein patterns were established by gel electrophoresis and reverse phase high performance liquid chromatography. The relatively higher amounts of p30 in particles with lower buoyant densities suggest that this protein is VP0 and is part of the immature picornavirion. The protein elution profiles obtained by HPLC were virtually identical for all the HAV strains examined but differed from those of other picornaviruses. The N-terminal amino acid sequence of VP1 and VP2 was determined and aligned to the nucleotide sequence. Sequencing VP0 and VP3 was not possible, probably because the amino termini are blocked. VP1, VP3, and VP0 induced specific antibodies in rabbits.