Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
29 04 2019
29 04 2019
Historique:
received:
13
02
2019
accepted:
28
03
2019
entrez:
1
5
2019
pubmed:
1
5
2019
medline:
14
5
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31036849
doi: 10.1038/s41467-019-09814-6
pii: 10.1038/s41467-019-09814-6
pmc: PMC6488583
doi:
Substances chimiques
Adhesins, Bacterial
0
Bacterial Outer Membrane Proteins
0
Escherichia coli Proteins
0
Glycosaminoglycans
0
Virulence Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1967Subventions
Organisme : NIH HHS
ID : S10 OD023681
Pays : United States
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