Imperial College London

Dr Tiago Costa

Faculty of Natural SciencesDepartment of Life Sciences

Senior Lecturer in Bacterial Pathogenesis
 
 
 
//

Contact

 

+44 (0)20 7594 3696t.costa Website

 
 
//

Location

 

5.02Sir Ernst Chain BuildingSouth Kensington Campus

//

Summary

 

Publications

Citation

BibTex format

@article{Hospenthal:2017:10.1016/j.str.2017.10.004,
author = {Hospenthal, MK and Zyla, D and Costa, TRD and Redzej, A and Giese, C and Lillington, J and Glockshuber, R and Waksman, G},
doi = {10.1016/j.str.2017.10.004},
journal = {Structure},
pages = {1829--1839.e4},
title = {The cryoelectron microscopy structure of the Type 1 chaperone-usher pilus rod},
url = {http://dx.doi.org/10.1016/j.str.2017.10.004},
volume = {25},
year = {2017}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable “spring-like” properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.
AU - Hospenthal,MK
AU - Zyla,D
AU - Costa,TRD
AU - Redzej,A
AU - Giese,C
AU - Lillington,J
AU - Glockshuber,R
AU - Waksman,G
DO - 10.1016/j.str.2017.10.004
EP - 1839
PY - 2017///
SN - 0969-2126
SP - 1829
TI - The cryoelectron microscopy structure of the Type 1 chaperone-usher pilus rod
T2 - Structure
UR - http://dx.doi.org/10.1016/j.str.2017.10.004
UR - https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000417092100007&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=a2bf6146997ec60c407a63945d4e92bb
UR - https://www.sciencedirect.com/science/article/pii/S0969212617303325?via%3Dihub
UR - http://hdl.handle.net/10044/1/103697
VL - 25
ER -