Structural highlights
FunctionBPPB3_BPT5 Forms the simplified baseplate, together with the p132 collar protein, the baseplate tube protein p140 and distal tail protein pb9. Closes the tail tube and, upon infection, opens to form a channel thereby anchoring the tube to the outer membrane. These changes allow the tape measure protein pb2 to be expelled and phage DNA to be transferred to the host. Also forms the start of the central straight fiber, which is continued with the straight fiber protein pb4.[1] Publication Abstract from PubMedMost 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 (Siphoviridae) 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 structures 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 undergone by T5 tail tip upon infection, which include bending of T5 central fiber on the side of the tail tip, tail anchoring 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. Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation.,Linares R, Arnaud CA, Effantin G, Darnault C, Epalle NH, Boeri Erba E, Schoehn G, Breyton C Sci Adv. 2023 Mar 24;9(12):eade9674. doi: 10.1126/sciadv.ade9674. Epub 2023 Mar , 24. PMID:36961893[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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