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Updated: Apr 11, 2026

Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
A "dock, lock, and latch" structural model for a staphylococcal adhesin binding to fibrinogen
Karthe Ponnuraj1, M Gabriela Bowden, Stacey Davis
1School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Staphylococcus epidermidis SdrG adhesin uses a novel "dock, lock, and latch" mechanism to bind human fibrinogen. This binding is crucial for bacterial attachment to biomaterials and may be common in Gram-positive bacteria.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- Gram-positive bacteria possess cell wall-anchored proteins mediating host interactions.
- Adhesins facilitate bacterial attachment to host tissues, crucial for infection.
- SdrG from Staphylococcus epidermidis binds fibrinogen, enabling attachment to biomaterials.
Purpose of the Study:
- To elucidate the structural basis of SdrG-fibrinogen interaction.
- To investigate the binding mechanism of the SdrG adhesin.
Main Methods:
- X-ray crystallography to determine the structure of SdrG and its complex with a fibrinogen peptide.
- Mutational studies of both SdrG and the fibrinogen peptide.
Main Results:
- Crystal structures revealed the ligand-binding region of SdrG.
- A dynamic "dock, lock, and latch" mechanism governs SdrG-ligand binding.
- Mutational analyses confirmed the proposed binding mechanism.
Conclusions:
- SdrG employs a unique "dock, lock, and latch" mechanism for fibrinogen binding.
- This mechanism is proposed as a general ligand-binding mode for related Gram-positive bacterial adhesins.
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