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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...
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Deciphering complement receptor type 1 interactions with recognition proteins of the lectin complement pathway.

Mickaël Jacquet1, Monique Lacroix, Sarah Ancelet

  • 1Commissariat à l'Energie Atomique, Institut de Biologie Structurale Jean-Pierre Ebel, 38027 Grenoble Cedex 1, France.

Journal of Immunology (Baltimore, Md. : 1950)
|March 6, 2013
PubMed
Summary
This summary is machine-generated.

This study reveals that mannan-binding lectin (MBL) and L-ficolin bind to complement receptor type 1 (CR1), identifying new interactions crucial for the lectin complement pathway and immune regulation.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Complement receptor type 1 (CR1) plays key roles in immune complex clearance and complement regulation.
  • CR1 interacts with complement components C3b and C4b, and potentially C1q and mannan-binding lectin (MBL).
  • The C-terminal region of CR1 (CCP22-30) is implicated in interactions with lectin pathway recognition proteins.

Purpose of the Study:

  • To investigate the interaction between human CR1 and recognition proteins of the lectin complement pathway, specifically MBL and ficolins.
  • To characterize the binding affinity and mapping of these interactions.

Main Methods:

  • Expression of a recombinant CR1 fragment (CCP22-30) in eukaryotic cells.
  • Surface plasmon resonance spectroscopy to assess binding kinetics.
  • Competition assays with MASP-3 and site-directed mutagenesis of MBL.

Main Results:

  • MBL and L-ficolin exhibit high-affinity binding to CR1 and its CCP22-30 fragment (nanomolar dissociation constants).
  • CR1 binding to MBL/L-ficolin occurs near the MASP binding site on the collagen stalks.
  • Mutation of a key lysine residue (K55) in MBL abolished CR1 binding.
  • The CR1 binding site was mapped to CCP24-25 within the D long homologous repeat.

Conclusions:

  • Ficolins represent novel ligands for CR1.
  • MBL and L-ficolin binding to CR1 involves ionic interactions between lysine residues on their collagen stalks and acidic residues on CR1 CCP24/25.