Role of complement S protein (vitronectin) in adherence of Streptococcus dysgalactiae to bovine epithelial cells

Dr Laerte F. Filippsen From the Institute of Bacteriology and Immunology, Faculty of Veterinary Medicine (Chhatwal, Filippsen, Valentin-Weigand, Blobel) and Clinical Research Unit for Blood Coagulation and Thrombosis of the Max-Planck-Gesellschaft (Preissner), Justus-Liebig-Universität, D-6300 Giessen, Federal Republic of Germany.

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Dr Peter Valentin-Weigand From the Institute of Bacteriology and Immunology, Faculty of Veterinary Medicine (Chhatwal, Filippsen, Valentin-Weigand, Blobel) and Clinical Research Unit for Blood Coagulation and Thrombosis of the Max-Planck-Gesellschaft (Preissner), Justus-Liebig-Universität, D-6300 Giessen, Federal Republic of Germany.

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Dr Hans Blobel From the Institute of Bacteriology and Immunology, Faculty of Veterinary Medicine (Chhatwal, Filippsen, Valentin-Weigand, Blobel) and Clinical Research Unit for Blood Coagulation and Thrombosis of the Max-Planck-Gesellschaft (Preissner), Justus-Liebig-Universität, D-6300 Giessen, Federal Republic of Germany.

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Klaus T. Preissner From the Institute of Bacteriology and Immunology, Faculty of Veterinary Medicine (Chhatwal, Filippsen, Valentin-Weigand, Blobel) and Clinical Research Unit for Blood Coagulation and Thrombosis of the Max-Planck-Gesellschaft (Preissner), Justus-Liebig-Universität, D-6300 Giessen, Federal Republic of Germany.

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Gursharan S. Chhatwal From the Institute of Bacteriology and Immunology, Faculty of Veterinary Medicine (Chhatwal, Filippsen, Valentin-Weigand, Blobel) and Clinical Research Unit for Blood Coagulation and Thrombosis of the Max-Planck-Gesellschaft (Preissner), Justus-Liebig-Universität, D-6300 Giessen, Federal Republic of Germany.

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Summary

The binding of bovine complement S protein (vitronectin) to Streptococcus dysgalactiae isolates from cattle with mastitis and the S protein's role in streptococcal adherence to bovine epithelial cells were investigated. All 25 clinical isolates of S dysgalactiae interacted with bovine S protein. None of the other streptococcal species tested bound to bovine S protein. The S protein-binding sites were saturable and highly sensitive to trypsin. The binding of bovine S protein to S dysgalactiae isolates was specific and could not be inhibited by other plasma proteins, such as fibronectin, albumin, fibrinogen, α2-macroglobulin, or IgG. Similarly, streptococcal binding of bovine S protein was not influenced by the synthetic peptide Gly-Arg-Gly-Asp-Ser, which constituted the host cell attachment sequence of S protein. In adherence experiments, prior binding of bovine S protein to S dysgalactiae enhanced streptococcal adherence to bovine epithelial cells. The enhancing effects by bovine S protein were abolished when the respective binding sites on the streptococci were digested by trypsin. Thus, bovine S protein could be an important mediator of adherence of S dysgalactiae to bovine epithelial cells.

Summary

The binding of bovine complement S protein (vitronectin) to Streptococcus dysgalactiae isolates from cattle with mastitis and the S protein's role in streptococcal adherence to bovine epithelial cells were investigated. All 25 clinical isolates of S dysgalactiae interacted with bovine S protein. None of the other streptococcal species tested bound to bovine S protein. The S protein-binding sites were saturable and highly sensitive to trypsin. The binding of bovine S protein to S dysgalactiae isolates was specific and could not be inhibited by other plasma proteins, such as fibronectin, albumin, fibrinogen, α2-macroglobulin, or IgG. Similarly, streptococcal binding of bovine S protein was not influenced by the synthetic peptide Gly-Arg-Gly-Asp-Ser, which constituted the host cell attachment sequence of S protein. In adherence experiments, prior binding of bovine S protein to S dysgalactiae enhanced streptococcal adherence to bovine epithelial cells. The enhancing effects by bovine S protein were abolished when the respective binding sites on the streptococci were digested by trypsin. Thus, bovine S protein could be an important mediator of adherence of S dysgalactiae to bovine epithelial cells.

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