期刊
SCIENCE ADVANCES
卷 9, 期 12, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.ade9674
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The structures of the T5 tail tip before and after interaction with its receptor, FhuA, have been determined using cryo-electron microscopy. These structures reveal important conformational changes, such as bending of the central fiber, anchoring of the tail to the membrane, opening of the tail tube, and formation of a transmembrane channel. This provides detailed insights into the initial steps of the infection mechanism.
Most bacteriophages present a tail allowing host recognition, cell wall perforation, and viral DNA channeling from the capsid to the infected bacterium cytoplasm. The majority of tailed phages bear a long flexible tail (Si-phoviridae) at the tip of which receptor binding proteins (RBPs) specifically interact with their host, triggering infection. In siphophage T5, the unique RBP is located at the extremity of a central fiber. We present the struc-tures of T5 tail tip, determined by cryo-electron microscopy before and after interaction with its E. coli receptor, FhuA, reconstituted into nanodisc. These structures bring out the important conformational changes under-gone by T5 tail tip upon infection, which include bending of T5 central fiber on the side of the tail tip, tail an-choring to the membrane, tail tube opening, and formation of a transmembrane channel. The data allow to detail the first steps of an otherwise undescribed infection mechanism.
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