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

Stubenrauch, Christopher, Belousoff, Matthew J., Hay, Iain D., Shen, Hsin-Hui, Lillington, James, Tuck, Kellie L., Peters, Kate M., Phan, Minh-Duy, Lo, Alvin, W., Schembri, Mark A., Strugnell, Richard A., Waksman, Gabriel and Lithgow, Trevor (2016) Effective assembly of fimbriae in Escherichia coli depends on the translocation assembly module nanomachine. Nature Microbiology, 1 7: 16064. doi:10.1038/nmicrobiol.2016.64


Author Stubenrauch, Christopher
Belousoff, Matthew J.
Hay, Iain D.
Shen, Hsin-Hui
Lillington, James
Tuck, Kellie L.
Peters, Kate M.
Phan, Minh-Duy
Lo, Alvin, W.
Schembri, Mark A.
Strugnell, Richard A.
Waksman, Gabriel
Lithgow, Trevor
Title Effective assembly of fimbriae in Escherichia coli depends on the translocation assembly module nanomachine
Formatted title
Effective assembly of fimbriae in Escherichia coli depends on the translocation assembly module nanomachine
Journal name Nature Microbiology   Check publisher's open access policy
ISSN 2058-5276
Publication date 2016-05-16
Year available 2016
Sub-type Letter to editor, brief commentary or brief communication
DOI 10.1038/nmicrobiol.2016.64
Open Access Status Not yet assessed
Volume 1
Issue 7
Start page 16064
Total pages 8
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
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 tissues(1-3). 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 platform called 'the usher' located in the outer membrane. Although the mechanism of pilus biogenesis is well characterized, how the usher itself is assembled at the outer membrane is unclear. Here, we report that a rapid response in usher assembly is crucially dependent on the translocation assembly module. We assayed the assembly reaction for a range of ushers and provide mechanistic insight into the β-barrel assembly pathway that enables the rapid deployment of bacterial fimbriae.
Formatted 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 platform called ‘the usher’ located in the outer membrane. Although the mechanism of pilus biogenesis is well characterized, how the usher itself is assembled at the outer membrane is unclear. Here, we report that a rapid response in usher assembly is crucially dependent on the translocation assembly module. We assayed the assembly reaction for a range of ushers and provide mechanistic insight into the β-barrel assembly pathway that enables the rapid deployment of bacterial fimbriae.
Q-Index Code CX
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Letter to editor, brief commentary or brief communication
Collections: HERDC Pre-Audit
School of Chemistry and Molecular Biosciences
 
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Created: Sun, 04 Sep 2016, 03:54:31 EST by Alvin Lo Wei Han on behalf of School of Chemistry & Molecular Biosciences