Premium
Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis
Author(s) -
Jiang Wangshu,
Ubhayasekera Wimal,
Pearson Melanie M.,
Knight Stefan D.
Publication year - 2018
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798318012391
Subject(s) - proteus mirabilis , fimbria , bacterial adhesin , microbiology and biotechnology , virulence , biology , chaperone (clinical) , biofilm , pathogenesis , virulence factor , fimbriae proteins , escherichia coli , bacteria , genetics , gene , immunology , medicine , pathology
The important uropathogen Proteus mirabilis encodes 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 two P. mirabilis fimbriae (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 of P. mirabilis fimbrial adhesins and their roles in the complex pathogenesis of urinary‐tract infections.