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Structural basis for Zn2+-dependent intercellular adhesion in staphylococcal biofilms.

Deborah G Conrady¹, Jeffrey J Wilson, Andrew B Herr

¹Department of Molecular Genetics, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.

Proceedings of the National Academy of Sciences of the United States of America

|January 2, 2013

Summary

This summary is machine-generated.

Staphylococcus bacteria form biofilms via Aap and SasG proteins, which self-associate with Zn(2+) to create cell adhesion. This study reveals the crystal structure of Aap, detailing its unique features for robust intercellular adhesion.

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Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

Staphylococcal bacteria, including Staphylococcus epidermidis and Staphylococcus aureus, are significant causes of chronic biofilm-related infections.
The proteins Aap (in S. epidermidis) and SasG (in S. aureus) are crucial for mediating biofilm formation in these bacteria.
The self-association of Aap and SasG, facilitated by Zn(2+), is essential for establishing extensive intercellular adhesion.

Purpose of the Study:

To determine the crystal structure of a Zn(2+)-bound construct from the self-associating region of the Aap protein.
To elucidate the structural mechanisms underlying Zn(2+)-dependent self-association and intercellular adhesion mediated by Aap.

Main Methods:

X-ray crystallography was employed to obtain the crystal structure of the Zn(2+)-bound Aap construct.
Analysis of multiple crystal forms to observe Zn(2+)-dependent dimer formation and coordination.

Main Results:

The crystal structure revealed unusual features, including elongated, solvent-exposed β-sheets and a lack of a canonical hydrophobic core.
Zn(2+)-dependent dimers of Aap were observed in three distinct crystal forms.
The formation of these dimers involves pleomorphic coordination of Zn(2+) across the dimer interface, facilitating trans-dimerization.

Conclusions:

The determined structures provide insights into how long, flexible surface proteins like Aap can form strong intercellular adhesion sites.
This mechanism is critical for bacterial survival and infection under challenging environmental conditions.
Understanding these structural details can inform strategies to combat biofilm-related staphylococcal infections.