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Invasion of Human Cells by a Bacterial Pathogen
Published on: March 21, 2011
Structural insight into binding of Staphylococcus aureus to human fibronectin
Ewa S Pilka1, Joern M Werner, Ulrich Schwarz-Linek
1Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
FEBS Letters
|December 27, 2005
Summary
Staphylococcus aureus proteins bind human fibronectin (Fn), causing a slight conformational change. This binding interaction results in an unusually extended structure of the bacterial protein when attached to Fn.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Staphylococcus aureus utilizes cell-wall proteins to bind human fibronectin (Fn).
- Understanding the structural basis of this interaction is crucial for deciphering bacterial adhesion mechanisms.
Purpose of the Study:
- To investigate the structural changes in fibronectin upon binding by Staphylococcus aureus proteins.
- To elucidate the conformation of fibronectin when engaged by bacterial adhesins.
Main Methods:
- Analysis of the intermodule interface between the 4F1 and 5F1 modules of fibronectin.
- Examination of beta-strand alignment and orientation during bacterial peptide binding.
Main Results:
- Bacterial peptide binding maintains the intermodule interface of fibronectin's N-terminal domain.
- A minor alteration in intermodule orientation and beta-strand alignment occurs.
- The 4F1 and 5F1 modules remain elongated, similar to the unbound state.
Conclusions:
- Staphylococcus aureus binding induces an unusual, highly extended conformation in fibronectin.
- Residues in both 4F1 and 5F1 modules are directly implicated in peptide binding.
- The findings support a model where bacterial proteins force fibronectin into an extended state.
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