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 () and Begoña Heras ()
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Jason J. Paxman: La Trobe University
Alvin W. Lo: The University of Queensland
Matthew J. Sullivan: Griffith University
Santosh Panjikar: Australian Synchrotron
Michael Kuiper: CSIRO
Andrew E. Whitten: Australian Nuclear Science and Technology Organisation
Geqing Wang: La Trobe University
Chi-Hao Luan: Northwestern University
Danilo G. Moriel: The University of Queensland
Lendl Tan: The University of Queensland
Kate M. Peters: The University of Queensland
Minh-Duy Phan: The University of Queensland
Christine L. Gee: Australian Synchrotron
Glen C. Ulett: Griffith University
Mark A. Schembri: The University of Queensland
Begoña Heras: La Trobe University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-09814-6

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