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Infection and Immunity, February 1999, p. 589-594, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Inhibition of Staphylococcus aureus Adherence to Collagen under Dynamic Conditions

Nehal Mohamed,1 Mark A. Teeters,1 Joseph M. Patti,2,dagger Magnus Höök,2 and Julia M. Ross1,*

Department of Chemical and Biochemical Engineering, University of Maryland Baltimore County, Baltimore, Maryland,1 and Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University, Houston, Texas2

Received 27 July 1998/Returned for modification 25 September 1998/Accepted 24 November 1998

Staphylococcus aureus is the most common etiological agent of bacterial arthritis and acute osteomyelitis and has been shown to bind to type II collagen under static and dynamic conditions. We have previously reported the effect of shear on the adhesion of S. aureus Phillips to collagen and found that this process is shear dependent (Z. Li, M. Höök, J. M. Patti, and J. M. Ross, Ann. Biomed. Eng. 24[Suppl. 1]:S-55). In this study, we used recombinant collagen adhesin fragments as well as polyclonal antibodies generated against adhesin fragments in attempts to inhibit bacterial adhesion. A parallel-plate flow chamber was used in a dynamic adhesion assay, and quantification of adhesion was accomplished by phase contrast video microscopy coupled with digital image processing. We report that both recombinant fragments studied, M19 and M55, and both polyclonal antibodies studied, alpha -M17 and alpha -M55, inhibit adhesion to varying degrees and that these processes are shear dependent. The M55 peptide and alpha -M55 cause much higher levels of inhibition than M19 and alpha -M17, respectively, at all wall shear rates studied. Our results demonstrate the importance of using a dynamic system in the assessment of inhibitory strategies and suggest the possible use of M55 and alpha -M55 in clinical applications to prevent infections caused by S. aureus adhesion to collagen.

* Corresponding author. Mailing address: Department of Chemical and Biochemical Engineering, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250. Phone: (410) 455-3414. Fax: (410) 455-1049. E-mail: jross{at}umbc.edu.

dagger Present address: Inhibitex Inc., Georgia State University, Department of Biology, Atlanta, GA.

Infection and Immunity, February 1999, p. 589-594, Vol. 67, No. 2
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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