A crystallographic approach to structural transitions in icosahedral viruses.

A crystallographic approach to structural transitions in icosahedral viruses.
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二十面体病毒结构转变的晶体学方法。

DOI:
10.1007/s00285-011-0425-5
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发表时间:
2012
影响因子:
1.9
通讯作者:
Indelicato G
Indelicato G
中科院分区:
数学4区
文献类型:
--
作者:
Indelicato G

文献摘要

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具有二十面体衣壳的病毒是所有病毒中最大的一类,包含许多重要的人类病原体,可以通过合适的二十面体3D准晶的二十面体不变的有限子集来建模。我们结合联合收割机的概念,从理论的三维准晶,并从晶体固体中的结构相变的理论,给出一个框架的二十面体病毒衣壳在成熟或感染过程中发生的结构转变的研究。由于3D准晶与6D二十面体Bravais晶格的合适子集一一对应,我们系统地研究了3D中经典Bain形变的6D类似物,其特征在于在中间构型处具有最小的对称性损失,并使用这些信息通过用于构建准晶的切割和投影方法来推断3D中假定的病毒衣壳过渡路径。我们将我们的方法应用到豇豆褪绿斑驳病毒(CCMV),并表明实验观察到的初始和最终CCMV结构之间的假定过渡路径最有可能保留一个三重轴。我们的程序提出了一个通用的方法,调查和预测的对称性约束的二十面体病毒的衣壳在结构转变过程中,从而提供了深入了解这些病原体的结构转变的机制。
Viruses with icosahedral capsids, which form the largest class of all viruses and contain a number of important human pathogens, can be modelled via suitable icosahedrally invariant finite subsets of icosahedral 3D quasicrystals. We combine concepts from the theory of 3D quasicrystals, and from the theory of structural phase transformations in crystalline solids, to give a framework for the study of the structural transitions occurring in icosahedral viral capsids during maturation or infection. As 3D quasicrystals are in a one-to-one correspondence with suitable subsets of 6D icosahedral Bravais lattices, we study systematically the 6D-analogs of the classical Bain deformations in 3D, characterized by minimal symmetry loss at intermediate configurations, and use this information to infer putative viral-capsid transition paths in 3D via the cut-and-project method used for the construction of quasicrystals. We apply our approach to the Cowpea Chlorotic Mottle virus (CCMV) and show that the putative transition path between the experimentally observed initial and final CCMV structures is most likely to preserve one threefold axis. Our procedure suggests a general method for the investigation and prediction of symmetry constraints on the capsids of icosahedral viruses during structural transitions, and thus provides insights into the mechanisms underlying structural transitions of these pathogens.