Abstract
Protein IIIa from human adenovirus 2 was shown to exist as a major soluble antigenic component in the infected cell pool of virus material when the cell extracts were analyzed in two-dimensional immunoelectrophoresis against hyperimmune antivirion sera. Protein IIIa was purified to apparent homogeneity by three methods, two using virus particles, one using infected cell lysates as starting material. The three methods gave similar yields of IIIa. Protein IIIa behaved as a spherical molecule with a sedimentation coefficient of 6.0 S, a frictional ratio of 1.02, and a molecular weight of 65,430 ± 1800 in its native state, suggestive of the existence of one single polypeptide unit. The N terminus of the IIIa was found to be glycine. The amino acid composition revealed an unusually high content of serine, glycine, and proline and a low content of lysine. Isoelectrophoretic analysis revealed a heterogeneous population with a major band at p I 5.95 and a minor band at p l 6.08. Only group-specific antigenic determinants were detected in IIIa, which did not seem to induce neutralizing antibodies.
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