Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules

Jason J. Paxman, Alvin W. Lo, Matthew J. Sullivan, Santosh Panjikar, Michael Kuiper, Andrew E. Whitten, Geqing Wang, Chi Hao Luan, Danilo G. Moriel, Lendl Tan, Kate M. Peters, Minh Duy Phan, Christine L. Gee, Glen C. Ulett, Mark A. Schembri, Begoña Heras*

*Corresponding author for this work

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter that is known to contribute to uropathogenic E. coli (UPEC) colonisation of the urinary tract. We provide evidence that UpaB can interact with glycosaminoglycans and host fibronectin. Unique modifications to its core β-helical structure create a groove on one side of the protein for interaction with glycosaminoglycans, while the opposite face can bind fibronectin. Our findings reveal far greater diversity in the autotransporter β-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.

Original languageEnglish (US)
Article number1967
JournalNature communications
Volume10
Issue number1
DOIs
StatePublished - Dec 1 2019

Fingerprint

Bacterial Adhesins
Macromolecules
macromolecules
proteins
infectious diseases
Glycosaminoglycans
Fibronectins
grooves
helices
bacteria
interactions
Uropathogenic Escherichia coli
membranes
crystal structure
Gram-Negative Bacteria
Urinary Tract
Escherichia coli
Bacteria
Membrane Proteins
Proteins

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

Cite this

Paxman, J. J., Lo, A. W., Sullivan, M. J., Panjikar, S., Kuiper, M., Whitten, A. E., ... Heras, B. (2019). Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. Nature communications, 10(1), [1967]. https://doi.org/10.1038/s41467-019-09814-6
Paxman, Jason J. ; Lo, Alvin W. ; Sullivan, Matthew J. ; Panjikar, Santosh ; Kuiper, Michael ; Whitten, Andrew E. ; Wang, Geqing ; Luan, Chi Hao ; Moriel, Danilo G. ; Tan, Lendl ; Peters, Kate M. ; Phan, Minh Duy ; Gee, Christine L. ; Ulett, Glen C. ; Schembri, Mark A. ; Heras, Begoña. / Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. In: Nature communications. 2019 ; Vol. 10, No. 1.
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Paxman, JJ, Lo, AW, Sullivan, MJ, Panjikar, S, Kuiper, M, Whitten, AE, Wang, G, Luan, CH, Moriel, DG, Tan, L, Peters, KM, Phan, MD, Gee, CL, Ulett, GC, Schembri, MA & Heras, B 2019, 'Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules', Nature communications, vol. 10, no. 1, 1967. https://doi.org/10.1038/s41467-019-09814-6

Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. / Paxman, Jason J.; Lo, Alvin W.; Sullivan, Matthew J.; Panjikar, Santosh; Kuiper, Michael; Whitten, Andrew E.; Wang, Geqing; Luan, Chi Hao; Moriel, Danilo G.; Tan, Lendl; Peters, Kate M.; Phan, Minh Duy; Gee, Christine L.; Ulett, Glen C.; Schembri, Mark A.; Heras, Begoña.

In: Nature communications, Vol. 10, No. 1, 1967, 01.12.2019.

Research output: Contribution to journalArticle

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