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Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein
Author(s) -
Lee WeiChao,
Matthews Steve,
Garnett James. A.
Publication year - 2016
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.2982
Subject(s) - fimbria , pilus , enteroaggregative escherichia coli , escherichia coli , microbiology and biotechnology , fimbriae proteins , biology , homology (biology) , sequence homology , homology modeling , peptide sequence , enterobacteriaceae , genetics , biochemistry , gene , enzyme
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.