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The Journal of biological chemistry2008; 283(25); 17615-17623; doi: 10.1074/jbc.M709844200

A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system.

Abstract: The M protein of Streptococcus equi subsp. equi known as fibrinogen-binding protein (FgBP) is a cell wall-associated protein with antiphagocytic activity that binds IgG. Recombinant versions of the seven equine IgG subclasses were used to investigate the subclass specificity of FgBP. FgBP bound predominantly to equine IgG4 and IgG7, with little or no binding to the other subclasses. Competitive binding experiments revealed that FgBP could inhibit the binding of staphylococcal protein A and streptococcal protein G to both IgG4 and IgG7, implicating the Fc interdomain region in binding to FgBP. To identify which of the two IgG Fc domains contributed to the interaction with FgBP, we tested two human IgG1/IgA1 domain swap mutants and found that both domains are required for full binding, with the CH3 domain playing a critical role. The binding site for FgBP was further localized using recombinant equine IgG7 antibodies with single or double point mutations to residues lying at the CH2-CH3 interface. We found that interaction of FgBP with equine IgG4 and IgG7 was able to disrupt C1q binding and antibody-mediated activation of the classical complement pathway, demonstrating an effective means by which S. equi may evade the immune response. The mode of interaction of FgBP with IgG fits a common theme for bacterial Ig-binding proteins. Remarkably, for those interactions studied in detail, it emerges that all the Ig-binding proteins target the CH2-CH3 domain interface, regardless of specificity for IgG or IgA, streptococcal or staphylococcal origin, or host species (equine or human).
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Publication Date: 2008-04-14 PubMed ID: 18411272PubMed Central: PMC2427354DOI: 10.1074/jbc.M709844200Google Scholar: Lookup
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  • Journal Article
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research article investigates how a specific bacterial protein (FgBP) from Streptococcus equi subsp. equi interacts with the immune system and the seven equine Immunoglobulin G (IgG) subclasses. The findings indicate that the protein primarily binds with equine IgG4 and IgG7 and its interaction interferes with the immune response, suggesting a common pattern for bacterial proteins interacting with immune cells.

Investigating the FgBP and Immunoglobulin Interaction

  • The researchers focused their study on a protein known as fibrinogen-binding protein (FgBP) which is found on the cell walls of the Streptococcus equi subsp. equi bacteria.
  • FgBP has antiphagocytic activities and is known to bind with Immunoglobulins (antibodies) particularly Immunoglobulin G(IgG).
  • In order to investigate this interaction, the researchers created recombinant versions of the seven different subclasses of equine IgG.
  • They then analyzed the specificity of FgBP in relation to these subclasses, concluding that FgBP predominantly binds to two specific subclasses: equine IgG4 and IgG7. There was little to no binding observed with the other five subclasses.

Examining the Competitive Binding of FgBP

  • To further understand the interaction, researchers conducted competitive binding experiments.
  • Findings revealed that FgBP could inhibit the binding of other bacterial proteins such as staphylococcal protein A and streptococcal protein G to IgG4 and IgG7.
  • This indicated that the specific region where FgBP binds to these subclasses is the Fc interdomain region.

Identifying the Interaction Domain

  • The researchers conducted experiments with the aim to identify which of the two IgG Fc domains contributed to the interaction with FgBP.
  • This involved testing two human IgG1/IgA1 domain swap mutants. Results indicated that both domains are necessary for full binding, however, the CH3 domain plays a more critical role.
  • Further experiments using recombinant equine IgG7 antibodies with single or double point mutations helped to localize the binding site for FgBP at the CH2-CH3 interface.

Impact on the Immune System

  • The study found that the interaction of FgBP with equine IgG4 and IgG7 disrupts C1q binding and prevents antibody-mediated activation of the classical complement pathway.
  • This indicates a method by which S. equi can evade the immune response, hence facilitating the persistence and spread of the bacteria.

Commonalities in Bacterial-Ig Interaction

  • The interaction of FgBP and IgG shows a common theme in how bacterial proteins interact with immune cells.
  • It emerges that all Ig-binding proteins target the CH2-CH3 domain interface, regardless of the specificity for IgG or IgA, their bacterial origin (streptococcal or staphylococcal), or the host species (equine or human).

Cite This Article

APA
Lewis MJ, Meehan M, Owen P, Woof JM. (2008). A common theme in interaction of bacterial immunoglobulin-binding proteins with immunoglobulins illustrated in the equine system. J Biol Chem, 283(25), 17615-17623. https://doi.org/10.1074/jbc.M709844200

Publication

The Journal of biological chemistry
ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 283
Issue: 25
Pages: 17615-17623

Researcher Affiliations

Lewis, Melanie J
  • Division of Pathology and Neuroscience, University of Dundee Medical School, Ninewells Hospital, Dundee DD19SY, United Kingdom.
Meehan, Mary
    Owen, Peter
      Woof, Jenny M

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Antibodies / chemistry
        • Bacterial Proteins / chemistry
        • Horses
        • Humans
        • Immunoglobulin A / chemistry
        • Immunoglobulin G / chemistry
        • Immunoglobulins / chemistry
        • Molecular Sequence Data
        • Recombinant Proteins / chemistry
        • Sequence Homology, Amino Acid
        • Species Specificity
        • Staphylococcus / metabolism
        • Streptococcus / metabolism

        Grant Funding

        • 074863 / Wellcome Trust

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        Citations

        This article has been cited 11 times.
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