Chai T J, Foulds J
J Bacteriol. 1979 Jan;137(1):226-33. doi: 10.1128/jb.137.1.226-233.1979.
Pure protein E, obtained after diethylaminoethyl-cellulose chromatography of ethylenediaminetetraacetic acid-Triton X-100-solubilized outer membrane proteins of Escherichia coli strain JF694, inactivated bacteriophage K3. Lipopolysaccharide enhanced bacteriophage inactivation. Antibody prepared against purified protein E protected bacteriophage K3 from inactivation by protein E. Bacteriophage K3 used a major outer membrane protein, protein II*, as part of its receptor. We conclude that proteins E and II* have a common region which interacts with bacteriophage K3. Protein E also inactivated two recently described bacteriophages, TC45 and TC23, that use protein E as at least part of their receptor.
从大肠杆菌菌株JF694的乙二胺四乙酸 - Triton X - 100增溶外膜蛋白经二乙氨基乙基纤维素层析获得的纯蛋白E可使噬菌体K3失活。脂多糖可增强噬菌体失活作用。针对纯化蛋白E制备的抗体可保护噬菌体K3不被蛋白E灭活。噬菌体K3将一种主要外膜蛋白,即蛋白II*,用作其受体的一部分。我们得出结论,蛋白E和蛋白II*具有与噬菌体K3相互作用的共同区域。蛋白E还可使另外两种最近描述的噬菌体TC45和TC23失活,这两种噬菌体至少将蛋白E用作其受体的一部分。