Autographa californica multiple nucleopolyhedrovirus GP64 protein: Analysis of domain I and V amino acid interactions and membrane fusion activity.
Autographa californica multiple nucleopolyhedrovirus GP64 protein: Analysis of domain I and V amino acid interactions and membrane fusion activity.
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DOI：
10.1016/j.virol.2015.11.025
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发表时间：
2016-01
期刊：
影响因子：
3.7
通讯作者：
Qianlong Yu;G. Blissard;Tong‐Xian Liu;Zhaofei Li
中科院分区：
文献类型：
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作者：
Qianlong Yu;G. Blissard;Tong‐Xian Liu;Zhaofei Li
苜蓿银纹夜蛾核型多角体病毒GP64是一种III类病毒融合蛋白。虽然GP64的融合后结构已被解决，但其融合前结构和构象变化的详细机制尚不清楚。在GP64中，预测结构域V与融合环2侧翼的两个结构域I片段相互作用。为了评估参与这些相互作用的氨基酸的意义，我们研究了24个氨基酸的位置，代表相互作用和保守的残基内域I和V.在几种情况下，取代一个单一的氨基酸参与预测的相互作用破坏膜融合活性，但没有一个氨基酸对似乎是绝对需要的。我们鉴定了结构域V中对膜融合重要的4个关键残基（G438、W439、T452和T456），以及似乎对GP 64的融合前构象的形成或稳定性重要的两个残基（G438和W439）。
TheAutographa californicamultiple nucleopolyhedrovirus GP64 is a class III viral fusion protein. Although the post-fusion structure of GP64 has been solved, its pre-fusion structure and the detailed mechanism of conformational change are unknown. In GP64, domain V is predicted to interact with two domain I segments that flank fusion loop 2. To evaluate the significance of the amino acids involved in these interactions, we examined 24 amino acid positions that represent interacting and conserved residues within domains I and V. In several cases, substitution of a single amino acid involved in a predicted interaction disrupted membrane fusion activity, but no single amino acid pair appears to be absolutely required. We identified 4 critical residues in domain V (G438, W439, T452, and T456) that are important for membrane fusion, and two residues (G438 and W439) that appear to be important for formation or stability of the pre-fusion conformation of GP64.