RT Journal Article
SR Electronic
T1 The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 164657
DO 10.1101/164657
A1 Manuela K. Hospenthal
A1 Tiago R. D. Costa
A1 Adam Redzej
A1 James Lillington
A1 Gabriel Waksman
YR 2017
UL http://biorxiv.org/content/early/2017/07/17/164657.abstract
AB 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 UPEC’s 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 UPEC’s ability to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2 Å 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.