Abstract
HUMAN adenovirus (Ad2), like many other viruses1, contains a virion-associated proteinase essential for the synthesis of infectious virus particles2–4. We observed proteinase activity in wild-type virus but not in the ts-1 virus2, which contains a mutation in the Ad2 L3 endoprotease gene5 that confers temperature-sensitive processing of virion precursor proteins. Unexpectedly, we did not observe proteinase activity with purified recombinant6,7 endoprotease protein (Mr 23 K). Purified recombinant endo-protease protein, however, complemented the mutation in ts-1 virions, restoring proteinase activity when mixed together. This implied that cofactors may be required. Here we reconstitute proteinase activity in vitro with three purified viral components: (1) the recombinant endoprotease protein; (2) an 11-amino-acid peptide that originates from the carboxy terminus of pVI, the precursor to virion component VI; and (3) adenovirus DNA. The use of DNA for a proteinase activity is unprecedented.
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Mangel, W., McGrath, W., Toledo, D. et al. Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Nature 361, 274–275 (1993). https://doi.org/10.1038/361274a0
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DOI: https://doi.org/10.1038/361274a0
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