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Publication Abstract from PubMed

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 A resolution) and AtfE (1.58 A 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.

Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis.,Jiang W, Ubhayasekera W, Pearson MM, Knight SD Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1053-1062. doi:, 10.1107/S2059798318012391. Epub 2018 Oct 29. PMID:30387764^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.