Matthews D A, Russell W C
Division of Cell and Molecular Biology, School of Biological and Medical Sciences, University of St Andrews, Fife, UK.
J Gen Virol. 1995 Aug;76 ( Pt 8):1959-69. doi: 10.1099/0022-1317-76-8-1959.
A variety of recombinant proteins derived from protein pVI of human adenovirus type 2 (Ad2) were analysed for their ability to bind Ad2 hexon in vitro. As pVI is also required for activation of the adenovirus-coded protease, the same pVI derivatives were assessed for their ability to activate recombinant adenovirus-coded 23K protease. Two regions, between amino acid residues 48-74 and 233-239 of pVI, were required for the interaction with hexon. These regions are highly conserved amongst mastadenovirus pVI proteins. Both these regions are capable on their own of binding hexon weakly but must be provided in cis for strong hexon binding. In addition, we found evidence to indicate than conformation as well as sequence was important for good hexon binding in our assays. Authentic processing of the appropriate recombinant pVI derivatives, by the recombinant protease, was obtained without the addition of other cofactors. These findings are discussed in relation to the role of pVI in triggering the adenovirus maturation pathway.
对源自人2型腺病毒(Ad2)pVI蛋白的多种重组蛋白进行了体外结合Ad2六邻体能力的分析。由于pVI对于腺病毒编码的蛋白酶的激活也是必需的,因此对相同的pVI衍生物激活重组腺病毒编码的23K蛋白酶的能力进行了评估。pVI与六邻体相互作用需要位于pVI氨基酸残基48 - 74和233 - 239之间的两个区域。这些区域在mastadenovirus pVI蛋白中高度保守。这两个区域自身都能够微弱地结合六邻体,但必须顺式存在才能实现与六邻体的强结合。此外,我们发现有证据表明在我们的实验中,构象以及序列对于良好的六邻体结合都很重要。在不添加其他辅助因子的情况下,通过重组蛋白酶对适当的重组pVI衍生物进行了真实的加工处理。本文结合pVI在触发腺病毒成熟途径中的作用对这些发现进行了讨论。