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Infection and immunity2005; 73(11); 7243-7251; doi: 10.1128/IAI.73.11.7243-7251.2005

Studies of fibronectin-binding proteins of Streptococcus equi.

Abstract: Streptococcus equi subsp. equi is the causative agent of strangles, a disease of the upper respiratory tract in horses. The initiation of S. equi subsp. equi infection is likely to involve cell surface-anchored molecules mediating bacterial adhesion to the epithelium of the host. The present study describes the cloning and characterization of FNEB, a fibronectin-binding protein with cell wall-anchoring motifs. FNEB can thus be predicted as cell surface located, contrary to the two previously characterized fibronectin-binding proteins in S. equi subsp. equi, FNE and SFS. Assays of antibody titers in horses and in experimentally infected mice indicate that the protein is immunogenic and expressed in vivo during S. equi subsp. equi infection. Using Western ligand blotting, it was shown that FNEB binds to the N-terminal 29-kDa fragment of fibronectin, while SFS and FNE both bind to the adjacent 40-kDa fragment. S. equi subsp. equi is known to bind fibronectin to a much lower degree than the closely related S. equi subsp. zooepidemicus, but the binding is primarily directed to the 29-kDa fragment. Inhibition studies using S. equi subsp. equi cells indicate that FNEB mediates cellular binding to fibronectin in this species.
Publication Date: 2005-10-22 PubMed ID: 16239519PubMed Central: PMC1273847DOI: 10.1128/IAI.73.11.7243-7251.2005Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

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The research studied fibronectin-binding proteins of Streptococcus equi, a bacterium that causes strangles, a disease of the horse’s upper respiratory tract. It identified and analyzed FNEB, a protein that binds to fibronectin and is expressed in vivo during infection, suggesting that it plays a significant role in the bacteria’s adhesive ability.

Fibronectin-binding Proteins in Strangles

  • The study focuses on Streptococcus equi subspecies equi, the bacterium responsible for strangles, an equine respiratory disease. Specifically, it investigates cell surface-anchored molecules that may be instrumental in bacterial adhesion to the host’s epithelium.
  • The research identifies a fibronectin-binding protein, FNEB, bearing cell wall-anchoring motifs. This suggests that it is located on the cell surface, unlike the previously characterized fibronectin-binding proteins in S. equi subspecies equi, FNE and SFS.

FNEB as an Immunogenic Protein

  • Antibody titer assays in infected horses and mice showed that FNEB is immunogenic, which means the protein induces an immune response. This immune response is further evidence of FNEB’s in vivo expression during infection, indicating its potential involvement in the disease process.

Detailed Characterization of FNEB

  • Using Western ligand blotting, the researchers found that FNEB binds to the N-terminal 29-kDa fragment of fibronectin. In contrast, the proteins SFS and FNE bind to an adjacent 40-kDa fragment.
  • S. equi subspecies equi has been known to have less fibronectin-binding capacity compared to the closely related S. equi subspecies zooepidemicus. However, its binding properties are primarily directed towards the 29-kDa fragment, suggesting a critical role of FNEB in this process.
  • Inhibition studies further confirmed that FNEB is essential in mediating cellular binding to fibronectin in S. equi subspecies equi.

Implications

  • This detailed investigation into the fibronectin-binding protein FNEB adds valuable knowledge to our understanding of the disease mechanisms in strangles. It suggests a potential therapeutic or preventative target, which can be further explored in the development of treatments or vaccines for this equine disease.

Cite This Article

APA
Lannergård J, Flock M, Johansson S, Flock JI, Guss B. (2005). Studies of fibronectin-binding proteins of Streptococcus equi. Infect Immun, 73(11), 7243-7251. https://doi.org/10.1128/IAI.73.11.7243-7251.2005

Publication

ISSN: 0019-9567
NlmUniqueID: 0246127
Country: United States
Language: English
Volume: 73
Issue: 11
Pages: 7243-7251

Researcher Affiliations

Lannergård, Jonas
  • Department of Microbiology, Swedish University of Agricultural Sciences, Box 7025, SE 750 07, Uppsala, Sweden. Jonas.Lannergard@mikrob.slu.se
Flock, Margareta
    Johansson, Staffan
      Flock, Jan-Ingmar
        Guss, Bengt

          MeSH Terms

          • Adhesins, Bacterial / chemistry
          • Adhesins, Bacterial / genetics
          • Adhesins, Bacterial / immunology
          • Adhesins, Bacterial / metabolism
          • Amino Acid Sequence
          • Animals
          • Binding Sites
          • Cloning, Molecular
          • Fibronectins / metabolism
          • Gene Expression Regulation, Bacterial
          • Genes, Bacterial / genetics
          • Horses / immunology
          • Immunoglobulin G / blood
          • Immunoglobulin G / immunology
          • Mice
          • Protein Binding
          • Sequence Alignment
          • Streptococcal Infections / immunology
          • Streptococcal Infections / microbiology
          • Streptococcus equi / chemistry
          • Streptococcus equi / cytology
          • Streptococcus equi / genetics
          • Streptococcus equi / metabolism
          • Substrate Specificity

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