Abstract
Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea in developing countries. They utilize aggregative adherence fimbriae (AAFs) to promote initial adherence to the host intestinal mucosa, promote the formation of biofilms, and mediate host invasion. Five AAFs have been identified to date and AAF/IV is amongst the most prevalent found in clinical isolates. Here we present the X‐ray crystal structure of the AAF/IV tip protein HdaB at 2.0 Å resolution. It shares high structural homology with members of the Afa/Dr superfamily of fimbriae, which are involved in host invasion. We highlight surface exposed residues that share sequence homology and propose that these may function in invasion and also non‐conserved regions that could mediate HdaB specific adhesive functions.
Highlights
Five aggregative adherence fimbriae (AAF) have been identified to date and AAF/IV is amongst the most prevalent found in clinical isolates
Enteroaggregative E. coli (EAEC) is the primary cause of pediatric diarrhea in developing countries[1,2] and its defining characteristic is an aggregative adherence (AA) pattern to HEp-2 cells in vitro,[1] which appear as a stacked brick-like arrangement of adherent bacteria
In 2011 a Shiga toxin (Stx)-producing strain of EAEC was responsible for a large outbreak in Germany, which spread across Europe and resulted in 3816 cases of gastroenteritis, 845 cases of hemolytic uremic syndrome (HUS), and 54 fatalities.[3,4,5]
Summary
This is a donor strand complemented construct (HdaB-dsA) and represents the structure of the HdaB domain in the final AAF/IV fiber. The first 10-residues (NTE) of the AAF/IV major subunit (HdaA) are fused after an artificial linker sequence to the C-terminus of HdaB.
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