Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi
Outer Membrane Proteins Ail and OmpF of Yersinia pestis Are Involved in the Adsorption of T7-Related Bacteriophage Yep-phi
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鼠疫耶尔森菌外膜蛋白Ail和OmpF参与T7相关噬菌体Yep-phi的吸附
DOI：
10.1128/jvi.01948-13
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发表时间：
2013-11-01
影响因子：
5.4
通讯作者：
Yang, Ruifu
中科院分区：
文献类型：
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作者：
Zhao, Xiangna;Cui, Yujun;Yang, Ruifu
Yep-phi是鼠疫耶尔森菌特有的t7相关噬菌体，在中国被常规用于鼠疫耶尔森菌的鉴定。在20摄氏度和37摄氏度的环境下，耶氏菌都会感染鼠疫耶尔森氏菌。无论生长温度如何，它在其他耶尔森氏菌中都没有活性。通过噬菌体吸附、噬菌体斑块形成、亲和层析和Western blot检测，鉴定出鼠疫菌il和OmpF的外膜蛋白除了粗脂多糖外，还参与了对Yep-phi的吸附。噬菌体尾部纤维蛋白特异性地与Ail和OmpF蛋白相互作用，其中518N、519N和523S残基是与OmpF相互作用所必需的，而518N、519N、522C和523S残基是与Ail相互作用所必需的。这是首次报道证明膜结合蛋白参与了t7相关噬菌体的吸附。这些观察结果突出了尾纤维蛋白在各种复杂噬菌体系统的进化和功能中的重要性，并为噬菌体-细菌相互作用提供了见解。
Yep-phi is a T7-related bacteriophage specific to Yersinia pestis, and it is routinely used in the identification of Y. pestis in China. Yep-phi infects Y. pestis grown at both 20 degrees C and 37 degrees C. It is inactive in other Yersinia species irrespective of the growth temperature. Based on phage adsorption, phage plaque formation, affinity chromatography, and Western blot assays, the outer membrane proteins of Y. pestis Ail and OmpF were identified to be involved, in addition to the rough lipopolysaccharide, in the adsorption of Yep-phi. The phage tail fiber protein specifically interacts with Ail and OmpF proteins, and residues 518N, 519N, and 523S of the phage tail fiber protein are essential for the interaction with OmpF, whereas residues 518N, 519N, 522C, and 523S are essential for the interaction with Ail. This is the first report to demonstrate that membrane-bound proteins are involved in the adsorption of a T7-related bacteriophage. The observations highlight the importance of the tail fiber protein in the evolution and function of various complex phage systems and provide insights into phage-bacterium interactions.