Biological and structural studies with an adenovirus type 2 temperature-sensitive mutant defective for uncoating.

We compared some of the biological and structural features of an adenovirus type 2 temperature-sensitive mutant (ts1) defective for maturation cleavages and uncoating with wild-type (WT) virus. The cleavage defect caused ts1 to produce virions at 39 degrees that contained five precursor proteins (pTP, 11K, PVI, PVII, PVIII). Coinfection of cells with such ts1 virions and a variety of mutants or WT virus not only failed to complement ts1 but actually depressed the infection by the second virus. The uncoating defect could only be overcome by multiplicity-dependent leakiness. The structure of the ts1 virion was compared with that of WT virus by iodination with chloramine-T, chloroglycoluril and lactoperoxidase, by cross-linking, and by digestion with proteases. Aside from the presence of precursor proteins and the greater stability of ts1 virions, no other differences were found that could account for the uncoating defect. Therefore, we postulate that this defect was caused by the greater stability imparted to the virion by precursor proteins PVI, PVII and PVIII.