Dr fimbrial adhesin (DraE) (DraE)

Dr haemagglutinin, primarily identified as the DraE subunit of Dr fimbriae, is a specialized surface adhesin expressed by uropathogenic Escherichia coli (UPEC) [3, 16]. It plays a critical role in the pathogenesis of urinary tract infections, such as pyelonephritis and cystitis, by mediating bacterial attachment to host tissues [3, 4]. Specifically, DraE recognizes and binds to the Dr blood group antigen located on Decay-accelerating factor (DAF, also known as CD55) and certain carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) on human epithelial cells [4, 7, 8]. This binding facilitates bacterial colonization of the uroepithelium and can lead to bacterial internalization, forming intracellular reservoirs that contribute to chronic or recurrent infections [4, 8]. Due to its essential role in infection, Dr haemagglutinin is considered a significant therapeutic target for anti-adhesion strategies and vaccine development [3, 8]. Research has demonstrated that specific molecules, including chloramphenicol, can competitively inhibit its binding to host receptors by mimicking the tyrosine-containing receptor moiety [7, 13].

Other names

Dr haemagglutininDr adhesinO75X adhesinAfaEDraE subunit

Inhibition of bacterial attachment to host cell receptors, specifically the Dr blood group antigen on Decay-accelerating factor (CD55) and carcinoembryonic antigen-related cell adhesion molecules (CEACAMs), thereby preventing tissue colonization and internalization [4, 13].