Influenza A M2 protein conformation depends on choice of model membrane.
Influenza A M2 protein conformation depends on choice of model membrane.
复制标题
DOI：
10.1002/bip.22617
复制
发表时间：
2015-07
期刊：
影响因子：
2.9
通讯作者：
Howard KP
中科院分区：
文献类型：
--
作者：
Saotome K;Duong-Ly KC;Howard KP
虽然存在甲型流感M2蛋白的晶体和NMR结构，但模型之间存在分歧。根据所采用的技术的要求，M2已经在一系列膜模拟物中进行了研究，包括洗涤剂胶束和脂质组成不同的膜双层。不同模型膜的使用使得对M2蛋白的全面理解所必需的已发表研究的结果的整合变得复杂。在这里，我们表明，使用定点自旋标记EPR光谱（SDSL-EPR）的膜双层中的M2肽的构象明显的双层的脂质组成的影响。改变双层膜内的双层厚度或侧压力分布改变观察到的M2构象。这里观察到的多种M2肽构象，以及在其他已发表的研究中，乐观地认为可以被认为是在流感感染期间的不同阶段由蛋白质采样的构象。然而，应该注意的是，在已发表的结构中观察到的异质性不仅仅是模型膜选择的人为因素。
While crystal and NMR structures exist of the influenza A M2 protein, there is disagreement between models. Depending on the requirements of the technique employed, M2 has been studied in a range of membrane mimetics including detergent micelles and membrane bilayers differing in lipid composition. The use of different model membranes complicates the integration of results from published studies necessary for an overall understanding of the M2 protein. Here we show using site-directed spin-label EPR spectroscopy (SDSL-EPR) that the conformations of M2 peptides in membrane bilayers are clearly influenced by the lipid composition of the bilayers. Altering the bilayer thickness or the lateral pressure profile within the bilayer membrane changes the M2 conformation observed. The multiple M2 peptide conformations observed here, and in other published studies, optimistically may be considered conformations that are sampled by the protein at various stages during influenza infectivity. However, care should be taken that the heterogeneity observed in published structures is not simply an artifact of the choice of the model membrane.