Journal article

Effective assembly of fimbriae in Escherichia coli depends on the translocation assembly module nanomachine

C Stubenrauch, MJ Belousoff, ID Hay, HH Shen, J Lillington, KL Tuck, KM Peters, MD Phan, AW Lo, MA Schembri, RA Strugnell, G Waksman, T Lithgow

Nature Microbiology | NATURE PUBLISHING GROUP | Published : 2016

Abstract

Outer membrane proteins are essential for Gram-negative bacteria to rapidly adapt to changes in their environment. Intricate remodelling of the outer membrane proteome is critical for bacterial pathogens to survive environmental changes, such as entry into host tissues1-3. Fimbriae (also known as pili) are appendages that extend up to 2 μm beyond the cell surface to function in adhesion for bacterial pathogens, and are critical for virulence. The best-studied examples of fimbriae are the type 1 and P fimbriae of uropathogenic Escherichia coli, the major causative agent of urinary tract infections in humans. Fimbriae share a common mode of biogenesis, orchestrated by a molecular assembly plat..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council


Funding Acknowledgements

The authors thank R. Goode and O. Kleinfeld for proteomic analysis and R. Bamert, R. Dunstan, R. Grinter and E. Heinz for comments on the manuscript. The authors also thank S. Hultgren for providing strain UTI89-P<INF>tet</INF>-fim. This work was supported by an NHMRC Program Grant (606788, to T.L. and R.A.S.) and an NHMRC Project grant (APP1042651, to M.A.S.). T.L. is an ARC Australian Laureate Fellow, MA. S. is an NHMRC Senior Research Fellow, H.H.S. is an ARC Super Science Fellow, M.J.B. is an NHMRC Biomedical Fellow, and I.D.H. is an ARC Laureate Postdoctoral Fellow.