Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
- Resource Type
- Academic Journal
- Authors
- Paxman JJ; Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia.; Lo AW; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.; Sullivan MJ; School of Medical Science, and Menzies Health Institute Queensland, Griffith University, Gold Coast, 4222, QLD, Australia.; Panjikar S; Macromolecular Crystallography, Australian Synchrotron, Clayton, 3168, VIC, Australia.; Department of Molecular Biology and Biochemistry, Monash University, Melbourne, 3800, VIC, Australia.; Kuiper M; Molecular & Materials Modelling group Data61, CSIRO, Docklands, Melbourne, 8012, VIC, Australia.; Whitten AE; Australian Centre for Neutron Scattering, Australian Nuclear Science and Technology Organisation, Lucas Heights, 2234, NSW, Australia.; Wang G; Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia.; Luan CH; High Throughput Analysis Laboratory and Department of Molecular Biosciences, Northwestern University, Chicago, 60208, IL, USA.; Moriel DG; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.; Tan L; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.; Peters KM; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.; Phan MD; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia.; Gee CL; Macromolecular Crystallography, Australian Synchrotron, Clayton, 3168, VIC, Australia.; Ulett GC; School of Medical Science, and Menzies Health Institute Queensland, Griffith University, Gold Coast, 4222, QLD, Australia.; Schembri MA; School of Chemistry and Molecular Biosciences, and Australian Infectious Diseases Research Centre, The University of Queensland, Brisbane, 4072, QLD, Australia. m.schembri@uq.edu.au.; Heras B; Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, 3086, VIC, Australia. b.heras@latrobe.edu.au.
- Source
- Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
- Subject
- Language
- English
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.