Role of Staphylococcus aureus protein A in adherence to silastic catheters.

J Surg Res

Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis, Minnesota 55455-0374, USA.

Published: May 2011

Background: Communities of bacteria, termed biofilms, frequently develop on central venous catheters, and bacterial contamination of central venous catheters is the most common cause of nosocomial bloodstream infections. Little is known about the initial events in bacterial adherence to the catheter surface, and experiments were designed to clarify the role of staphylococcal protein A, serum, and immunoglobulin in adherence of Staphylococcus aureus to silastic catheters. We hypothesized that S. aureus protein A in the presence of serum and immunoglobulin would alter S. aureus adherence to silastic catheters.

Materials And Methods: Three strains of S. aureus with varying expression of staphylococcal protein A were incubated 15 min at room temperature with silastic catheters, and bacterial adherence to the catheter surface was quantified. In addition, the effects of serum, albumin, and purified IgG on bacterial adherence were assessed.

Results: Both serum and albumin had an inhibitory effect on S. aureus adherence to the catheter surface, and protein A expression did not appreciably modulate these effects. Purified serum IgG also inhibited S. aureus adherence, with IgG having a greater inhibitory effect on the adherence of an S. aureus strain deficient in protein A compared with an S. aureus strain expressing high levels of protein A.

Conclusion: S. aureus adherence to silastic catheters was inhibited by whole serum, albumin, and purified IgG. Expression of staphylococcal protein A interfered with IgG mediated inhibition of bacterial binding to the catheter surface. Protein A altered S. aureus adherence to silastic catheters in the presence of immunoglobulin, but not in the presence of serum or albumin.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3240895PMC
http://dx.doi.org/10.1016/j.jss.2010.12.039DOI Listing

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