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An atomic resolution model for assembly, architecture, and function of the Dr adhesins
Kirstine L Anderson1, Jason Billington, David Pettigrew
1Department of Biological Sciences, Wolfson Laboratories, Imperial College London, South Kensington, London SW7 2AZ, United Kingdom.
Molecular Cell
|August 26, 2004
Summary
The Dr family of Escherichia coli adhesion proteins, unlike others, causes both diarrheal and urinary tract infections. Their structural model reveals how they assemble and form surface fibers to target host cells.
Area of Science:
- Microbiology
- Structural Biology
- Pathogenesis
Background:
- Pathogenic bacteria utilize adhesion protein complexes to infect host cells.
- The Dr family of Escherichia coli adhesion proteins is unique, causing both diarrheal and urinary tract infections.
- These proteins target the decay-accelerating factor (DAF or CD55) receptor on host cells.
Purpose of the Study:
- To elucidate the structural basis for the assembly and architecture of Dr family adhesion proteins.
- To understand how these proteins form both fimbrial and afimbrial structures.
Main Methods:
- Utilized a newly solved three-dimensional structure of AfaE.
- Constructed a robust atomic resolution model.
Main Results:
- Revealed the structural basis for assembly via donor strand complementation.
- Elucidated the architecture of capped surface fibers formed by these proteins.
Conclusions:
- The structural model provides insights into the assembly mechanism of Dr family adhesins.
- Understanding the structure of AfaE is crucial for comprehending the pathogenesis of infections caused by this bacterial family.