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

DOI: 10.1002/pro.2982 DOI Help

Authors: Wei-Chao Lee (Imperial College London) , Steve Matthews (Imperial College London) , James A. Garnett (Queen Mary University London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Protein Science

State: Published (Approved)
Published: July 2016
Diamond Proposal Number(s): 12579

Open Access Open Access

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.

Diamond Keywords: Bacteria; Gastroenteritis

Subject Areas: Biology and Bio-materials

Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 14/09/2016 10:27


Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)