Department of Cell and Molecular Biology, Uppsala University, Biomedical Center, PO Box 596, SE-751 24 Uppsala, Sweden.
Department of Microbiology and Immunology, University of Michigan Medical School, 5641 Medical Science Building II, 1150 West Medical Center Drive, Ann Arbor, MI 48109-0620, USA.
Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1053-1062. doi: 10.1107/S2059798318012391. Epub 2018 Oct 29.
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.
重要的尿路病原体奇异变形杆菌编码了数量创纪录的伴侣蛋白/usher 途径黏附菌毛。这些菌毛用于黏附细胞表面/组织和生物膜形成，通常是细菌发病机制中重要的毒力因子。在这里，呈现了来自两种奇异变形杆菌菌毛（UCA/NAF 和 ATF）的顶端双结构域黏附素 UcaD（1.5Å 分辨率）和 AtfE（1.58Å 分辨率）的受体结合结构域的结构。UcaD 和 AtfE 的结构均类似于 F17G 型顶端定位菌毛受体结合结构域，尽管序列相似性有限，但结构非常相似。这些结构代表了朝着理解奇异变形杆菌菌毛黏附素及其在尿路感染复杂发病机制中的作用的分子水平理解迈出的重要一步。
