Conformational changes of short tail fibers enable genome delivery of Podoviridae phage SU10 (RICCEM-2021)
| Authors | |
|---|---|
| Year of publication | 2021 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
| Citation | |
| Description | Phage SU10, infecting Escherichia coli, belongs to the family Podoviridae of phages with short non-contractile tails. The tails enable Podoviridae phages to attach at a cell surface and penetrate bacterial cell wall. However, there is limited information about conformational changes of tails of Podoviridae phages that are required for infection of a cell. We used cryo-electron microscopy to determine the structures of virion and genome release intermediate of phage SU10. The virion of SU10 is formed by a prolate capsid and a tail attached to a dodecameric portal complex. The tail, which is formed by a dodecamer of adaptor proteins, hexamer of tail proteins, and trimer of tail needle proteins, is decorated by long and short fibers. SU10 uses the long tail fibers for initial attachment to a cell. The binding of short tail fibers to a bacterial surface requires their rotation by 135°, which is connected to straightening of tail proteins. In the new conformation, the short tail fibers and tail proteins alternate to form a 20 nm long nozzle. Attachment of short tail fibers to the cell surface forces the tail needle, which protrudes from the tail nozzle, through the outer membrane of the bacterial cell. To open the tail channel, the tail needle dissociates from the baseplate. The head of SU10 contains inner core proteins that have a predicted transglycosylase activity to degrade cell wall peptidoglycan and may also attach to the tail nozzle to extend it across periplasm and inner membrane into bacterial cytoplasm. The nozzle with the putative extension formed by inner core proteins enable ejection of SU10 DNA into bacterial cytoplasm |
| Related projects: |