Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.
Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials.
复制标题
噬菌体 P22 外壳蛋白 C 末端的位置为衣壳材料的设计提供了机会。
DOI：
10.1021/bm400796c
复制
发表时间：
2013
影响因子：
6.2
通讯作者：
Douglas,Trevor
中科院分区：
文献类型：
--
作者：
Servid,Amy;Jordan,Paul;O'Neil,Alison;Prevelige,Peter;Douglas,Trevor
用于未来治疗和材料应用的病毒样颗粒 (VLP) 内表面和外表面修饰的合理设计基于衣壳的结构信息。现有的基于冷冻电子显微镜的模型表明，噬菌体 P22 外壳蛋白 (CP) 的 C 末端向衣壳外部延伸。我们通过 C 末端遗传操作进行的生化分析支持 CP C 末端暴露在 P22 衣壳外部的模型。显示附加到 CP C 末端的 6xHis 标签的衣壳与 Ni 亲和柱结合，向衣壳中添加带正电或带负电的卷曲螺旋肽会导致这些衣壳在混合时缔合。此外，附加到 CP C 末端的单个半胱氨酸会导致衣壳间二硫键的形成，并可作为化学修饰的位点。因此，C 末端是肽多价展示的重要位置，有助于纳米级组装和衣壳修饰。
Rational design of modifications to the interior and exterior surfaces of virus-like particles (VLPs) for future therapeutic and materials applications is based on structural information about the capsid. Existing cryo-electron microscopy-based models suggest that the C-terminus of the bacteriophage P22 coat protein (CP) extends toward the capsid exterior. Our biochemical analysis through genetic manipulations of the C-terminus supports the model where the CP C-terminus is exposed on the exterior of the P22 capsid. Capsids displaying a 6xHis tag appended to the CP C-terminus bind to a Ni affinity column, and the addition of positively or negatively charged coiled coil peptides to the capsid results in association of these capsids upon mixing. Additionally, a single cysteine appended to the CP C-terminus results in the formation of intercapsid disulfide bonds and can serve as a site for chemical modifications. Thus, the C-terminus is a powerful location for multivalent display of peptides that facilitate nanoscale assembly and capsid modification.