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Binding of human complement component C4b-binding protein (C4BP) to Streptococcus pyogenes involves the C4b-binding

P Accardo1, P Sánchez-Corral, O Criado

  • 1Department of Immunology, Center for Biological Research, CSIC, Madrid, Spain.

Journal of Immunology (Baltimore, Md. : 1950)
|December 1, 1996
PubMed
Summary

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Streptococcus pyogenes evades the immune system by mimicking human complement protein C4b. This molecular mimicry allows bacteria to bind human C4b-binding protein (hC4BP), hindering pathogen elimination.

Area of Science:

  • Immunology
  • Microbiology
  • Molecular Biology

Background:

  • The complement system is crucial for eliminating pathogens via C3b and C4b protein deposition.
  • Pathogens like Streptococcus pyogenes possess mechanisms to evade host complement defenses.

Purpose of the Study:

  • To elucidate the molecular mechanism by which Streptococcus pyogenes interacts with human C4b-binding protein (hC4BP).
  • To understand how this interaction impacts complement deposition on the bacterial surface.

Main Methods:

  • Investigated the binding interaction between streptococcal surface molecules and hC4BP.
  • Characterized the specific binding site on hC4BP involved in the interaction.

Main Results:

  • Streptococcal surface molecules bind to hC4BP at a site identical to the C4b binding site.

Related Experiment Videos

  • The interaction involves multiple binding surfaces within the short consensus repeats 1-3 of hC4BP's alpha-chain.
  • Conclusions:

    • Streptococcus pyogenes employs molecular mimicry, presenting surface structures that resemble human C4b epitopes.
    • This mimicry facilitates binding to hC4BP, potentially downregulating complement-mediated bacterial clearance.