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- Title
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
- Authors
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
- 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. Autotransporter proteins are localised to the bacterial surface and promote colonisation of host epithelial surfaces. Here, the authors present the crystal structure of autotransporter UpaB and show evidence for distinct binding sites for glycosaminoglycans and host fibronectin.
- Publication
Nature Communications, 2019, Vol 10, Issue 1, pN.PAG
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-019-09814-6