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Adenoviruses encode a cysteine protease, adenain, required for uncoating and virion maturation. Adenain activity is regulated by an 11-amino-acid peptide cofactor thiol-bonded distal to the active site. Structural and experimental data suggest that the peptide might stabilize adenain in an optimal conformation for enzyme activity by bridging two noncontiguous regions of the molecule. The sequence...
Based on the alignment of 12 adenovirus protease sequences, we have identified eleven conserved residues for mutagenesis. Eight of these, E5, D26, N44, E71, D77, D102, N144, and N170, are potential candidates for the third residue of the active site triad. N44, E71, N144, and N170 proved to be essential for enzyme activity. Glutamic acid 71 was proposed for the active site. Mutation of the three conserved...
The catalytic activity of the adenovirus cysteine peptidase is increased by a specific 11-amino-acid peptide adduct (GVQSLKRRRCF, referred to as pVIc). To identify additional peptides which might bind and alter the activity of the protease, a cysteine-constrained random peptide phage library was screened. Of 29 different phages which were isolated, 7 contained the consensus sequence VEGGS. Despite...
We have analyzed the mechanisms used by adenovirus to gain entry into the host cell. Using both virus infection and the ability of adenovirus particles to enhance polylysine/DNA uptake as a measure of virus entry, we have demonstrated that the adenovirus-encoded 23K protease is required for two functions in the infection process. A proteolytic processing of the capsid is required to generate a virus...
Infection with the adenovirus type 2 ts1 mutant at the nonpermissive temperature resulted in the production of noninfectious virions. This has been ascribed to the P137L mutation in the virus-encoded cysteine protease which causes a defect in protease activity. Here we have examined the ts1 defect in detail as a means of learning more about the viral protease. The ts1 protease accumulated in the nucleus...
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