Journal
NATURE COMMUNICATIONS
Volume 10, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-019-09814-6
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Funding
- Australian Research Council (ARC) [DP150102287, DP180102987]
- La Trobe University Research Focus Area Understanding Disease Express Grant
- Victorian Life Sciences Computation Initiative grant [LTU0011]
- ARC Future Fellowship [FT130100580]
- Australian National Health and Medical Research Council Senior Research Fellowship [GNT1106930]
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Autotransporters are the largest family of outer membrane and secreted proteins in Gramnegative 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 beta-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 beta-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.
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