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Redzej, A.

Publications and source records attributed to Redzej, A..

2 recordsLinked to original sources

Cryo-EM Structure of the R388 plasmid conjugative pilus reveals a helical polymer characterised by an unusual pilin/phospholipid binary complex

Bacterial conjugation is a process by which DNA is transferred unidirectionally from a donor cell to a recipient cell. It is the main means by which antibiotics resistance genes spread among bacterial populations. It is crucially dependent upon the elaboration of an extracellular appendage, termed "pilus", by a large double-membrane spanning secretion system termed conjugative "type IV secretion system". Here we present the structure of the conjugative pilus encoded by the R388 plasmid. We demonstrate that, as opposed to all conjugative pili produced so far for cryo-EM structure determination, that encoded by the R388 plasmid is greatly stimulated by the presence of recipient cells. Comparison of its cryo-EM structure with existing conjugative pilus structures highlights a number of important differences between the R388 pilus structure and that of its homologues, the most prominent being the highly distinctive conformation of its bound lipid.

microbiology↗

The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod

Chaperone-usher pili are long, polymeric protein fibres displayed on the surface of many bacterial pathogens. These critical virulence factors allow bacteria to specifically attach to host cells during infection. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during UPECs colonisation of the urinary tract, mediating bacterial attachment to the bladder and kidney, respectively. Also, their biomechanical properties that allow them to reversibly uncoil in response to flow-induced forces are critical for UPECs ability to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2 [A] resolution cryo-electron microscopy (cryo-EM) structure of the type 1 pilus rod, which together with the previous structure of the P pilus rod, enables us to understand the remarkable \"spring-like\" properties of chaperone-usher pili in more detail.

molecular biology↗