We compared some of the biological and structural features of an adenovirus type 2 temperature-sensitive mutant (tsl) defective for maturation cleavages and uncoating with wild-type (WT) virus. The cleavage defect caused tsl to produce virions at 39° that contained five precursor proteins (pTP, UK, PVI, PVΠ, PVIII). Coinfection of cells with such tsl virions and a variety of mutants or WT virus not only failed to complement tsl but actually depressed the infection by the second virus. The uncoating defect could only be overcome by multiplicity-dependent leakiness. The structure of the tsl 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 tsl 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, PVΠ and PVIII.

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