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Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein

Research output: Contribution to journalArticle

Wei Chao Lee, Steve Matthews, James A. Garnett

Original languageEnglish
Pages (from-to)1898-1905
Number of pages8
JournalProtein science
DOIs
Publication statusPublished - 1 Oct 2016

King's Authors

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.

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