Abstract
Staphylococcus epidermidis is the leading cause of device-related infections. These infections require an initial colonization step in which S. epidermidis adheres to the implanted material. This process is usually mediated by specific bacterial surface proteins and host factors coating the foreign device. Some of these surface proteins belong to the serine-aspartate repeat (Sdr) family, which includes adhesins from Staphyloccus aureus and S. epidermidis. Using a heterologous expression system in Lactococcus lactis to overcome possible staphylococcal adherence redundancy we observed that one of these Sdr proteins, SdrF, mediates binding to type I collagen when present on the lactococcal cell surface. We used lactococcal recombinant strains, a protein-protein interaction assay and Western ligand blot analysis to demonstrate that this process occurs via the B domain of SdrF and both the alpha1 and alpha2 chains of type I collagen. It was also found that a single B domain repeat of S. epidermidis 9491 retains the capacity to bind to type I collagen. We demonstrated that the putative ligand binding N-terminal A domain does not bind to collagen which suggests that SdrF might be a multiligand adhesin. Antibodies directed against the B domain significantly reduce in vitro adherence of S. epidermidis to immobilized collagen.
Highlights
The pathogenesis of these infections is complex and involves a wide range of interactions between bacterial and host factors
Presence of SdrF on the Cell Surface of L. lactis Elicits Adherence to Type I Cn—As mentioned above, our laboratory recently found that SdrF from S. epidermidis mediated adhesion to patient-explanted ventricular assist devices (VADs) drivelines when expressed and exported onto the lactococcal cell surface
L. lactis pOri-SdrF cells showed better binding capacity compared with S. epidermidis 9491, which might be explained by an increase in the presence of SdrF on the lactococcal cell surface as suggested by flow cytometry analysis
Summary
F-HisA5Bam, F-HisA3Pst F-HisB5Bam, F-HisB3Pst lukS-5Bam, lukS-3Pst F-HisB5Bam, QEB1-3Pst QEB2-5Bam, QEB2-3Pst QEB3-5Bam, QEB3-3Pst QEB4-5Bam, F-HisB3Pst. L. lactis cell surface expression L. lactis cell surface expression L. lactis cell surface expression L. lactis cell surface expression. Ested in identifying the specific ligand for SdrF as well as characterizing its binding mechanisms. We report that SdrF binds to Cn type I. This binding appears to be mediated by the B domain
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