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J Virol. 1973 August; 12(2): 241-252
Copyright © 1973 American Society for Microbiology. All Rights Reserved.

Processing of Adenovirus 2-Induced Proteins

C. W. Anderson, P. R. Baum and R. F. Gesteland

1 Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724

ABSTRACT

Analysis of 35S-methionine-labeled extracts of adenovirus 2-infected KB cells revealed 22 virus-induced polypeptide components. Most proteins of the virion were easily detected in extracts of whole cells labeled for short periods between 15 and 30 h after infection; however, several virion components were conspicuously absent. Radioactivity appeared in two of these virion components during a chase in nonradioactive medium, and this appearance was paralleled by a decrease in the radioactivity associated with two nonvirion adenovirus-induced proteins, results which imply precursor-product relationships for these components. Comparison of one of the chasable adenovirus-induced components (designated P-VII; mass of 20,000 daltons) and the major core protein (VII; mass of 18,500 daltons) of the virion showed that they have four common methionine-containing tryptic peptides; P-VII has an additional methionine residue which is not found in the major core protein. We propose that at least two of the adenovirus 2 virion components are derived by the cleavage of higher molecular weight precursor polypeptides.

J Virol. 1973 August; 12(2): 241-252
Copyright © 1973 American Society for Microbiology. All Rights Reserved.



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