Structural proteins of adenoviruses. X. Isolation and topography of low molecular weight antigens from the virion of adenovirus type 2.

Abstract

Abstract With high resolution SDS-polyacrylamide gel electrophoresis ( Maizel, 1971 ) and a new method to extract the basic proteins, it was ascertained that adenovirus type 2 contains at least 10 distinct polypeptides (II, III, IIIa, IV–X) and possibly more. Five proteins (V, VI, VII, VIII, and X) were purified by selective extraction in urea at high ionic strength, and low pH followed by preparative polyacrylamide electrophoresis toward the cathode at pH 3.4. Antisera, produced against proteins V, VI, and VII were used to reveal that these proteins were antigenically distinct and unrelated to hexons, pentons, and fibers. The location of the polypeptides was investigated by two methods of virion degradation ( Prage et al. , 1970 ). Polypeptides V and VII were associated with the DNA-containing core. Polypeptide VI appeared to be associated with all hexons of the virion. Hexons from the triangular facets of the capsid contained in addition to polypeptides II and VI, polypeptide IX, and possibly also polypeptide VIII. Hexons purified from infected cells contained only polypeptide II. Polypeptide IIIa was preferentially released together with the peripentonal hexons.