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Related Experiment Video

Updated: Jul 15, 2026

Invasion of Human Cells by a Bacterial Pathogen

Invasion of Human Cells by a Bacterial Pathogen

Published on: March 21, 2011

SdrF, a Staphylococcus epidermidis surface protein, binds type I collagen.

Carlos Arrecubieta¹, Mei-Ho Lee, Alistair Macey

¹Division of Infectious Diseases, Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.

The Journal of Biological Chemistry

|May 3, 2007

Summary

Staphylococcus epidermidis uses SdrF surface protein to bind to collagen, a key step in device infections. Antibodies targeting SdrF

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Area of Science:

Microbiology
Infectious Diseases
Biochemistry

Background:

Staphylococcus epidermidis is a primary cause of device-related infections.
Bacterial adherence to implanted materials is crucial for infection initiation.
Serine-aspartate repeat (Sdr) proteins are key bacterial adhesins.

Purpose of the Study:

To investigate the role of SdrF in Staphylococcus epidermidis adherence to medical devices.
To identify the specific domains of SdrF involved in collagen binding.

Main Methods:

Utilized a Lactococcus lactis heterologous expression system.
Employed protein-protein interaction assays and Western ligand blot analysis.
Tested binding of SdrF domains to type I collagen chains.

Main Results:

SdrF mediates Staphylococcus epidermidis binding to type I collagen via its B domain.
Both alpha1 and alpha2 chains of type I collagen bind to the SdrF B domain.
Antibodies against the SdrF B domain significantly reduced bacterial adherence to collagen.

Conclusions:

SdrF is a collagen-binding adhesin critical for Staphylococcus epidermidis colonization.
The SdrF B domain is responsible for collagen interaction, suggesting a multiligand adhesin.
Targeting SdrF offers a potential strategy to prevent device-related infections.