Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogenProteus mirabilis

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Abstract
The important uropathogenProteus mirabilisencodes a record number of chaperone/usher-pathway adhesive fimbriae. Such fimbriae, which are used for adhesion to cell surfaces/tissues and for biofilm formation, are typically important virulence factors in bacterial pathogenesis. Here, the structures of the receptor-binding domains of the tip-located two-domain adhesins UcaD (1.5 Å resolution) and AtfE (1.58 Å resolution) from twoP. mirabilisfimbriae (UCA/NAF and ATF) are presented. The structures of UcaD and AtfE are both similar to the F17G type of tip-located fimbrial receptor-binding domains, and the structures are very similar despite having only limited sequence similarity. These structures represent an important step towards a molecular-level understanding ofP. mirabilisfimbrial adhesins and their roles in the complex pathogenesis of urinary-tract infections.
Funding Information
  • Vetenskapsrådet (2016-04451)
  • U.S. Public Health Service (AI083743)

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