Zwizinski C, Wickner W
Biochim Biophys Acta. 1977 Dec 1;471(2):169-76. doi: 10.1016/0005-2736(77)90247-4.
The major capsid protein of M13 bacteriophage is incorporated at each stage of infection into the host plasma membrane with its amino terminus exposed on the outer surface. Purified M13 coat protein is incorporated with the same asymmetry into synthetic phosphatidylcholine vesicles formed near the Tm of the lipid by a cholate dilution technique. We now report that the lipid in the pre-dilution mixture exists as mixed micelles of uniform size. Prior to dilution, the coat protein is present in at least two states of aggregation, both of which behave similarly in the model membrane assembly reaction. No detectable lipid-protein interaction occurs prior to dilution. Upon dilution there is rapid production of small closed vesicles and coat protein is converted to a chymotrypsin-resistant form, presumably reflecting its incorporation into these vesicle bilayers. Formation of large (greater than 6000 A diameter) vesicles occurs slowly with preservation of coat protein asymmetry and internal volume. A model for this assembly reaction is proposed.
M13噬菌体的主要衣壳蛋白在感染的每个阶段都整合到宿主质膜中，其氨基末端暴露在外表面。纯化的M13衣壳蛋白以相同的不对称方式整合到通过胆酸盐稀释技术在脂质的熔点附近形成的合成磷脂酰胆碱囊泡中。我们现在报告，预稀释混合物中的脂质以大小均匀的混合胶束形式存在。在稀释之前，衣壳蛋白以至少两种聚集状态存在，这两种状态在模型膜组装反应中的行为相似。在稀释之前未检测到脂质-蛋白质相互作用。稀释后，迅速产生小的封闭囊泡，并且衣壳蛋白转化为胰凝乳蛋白酶抗性形式，大概反映了它整合到这些囊泡双层中。大（直径大于6000 Å）囊泡的形成缓慢，同时保留衣壳蛋白的不对称性和内部体积。提出了这种组装反应的模型。
