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Related Experiment Videos

Complement receptor 1/CD35 is a receptor for mannan-binding lectin.

I Ghiran1, S F Barbashov, L B Klickstein

  • 1Harvard-Thorndike Laboratory, Division of Allergy and Inflammation, Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA.

The Journal of Experimental Medicine
|December 20, 2000
PubMed
Summary
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Mannan-binding lectin (MBL) binds to complement receptor 1 (CR1), acting as its cellular receptor. This discovery clarifies MBL

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • Mannan-binding lectin (MBL) is a collectin with opsonic function.
  • The cellular receptor for MBL has not been previously identified.
  • Complement C1q, homologous to MBL, binds to complement receptor 1 (CR1/CD35).

Purpose of the Study:

  • To investigate if complement receptor 1 (CR1) functions as a cellular receptor for Mannan-binding lectin (MBL).

Main Methods:

  • Investigated MBL binding to recombinant soluble CR1 (sCR1) using radioiodinated MBL.
  • Assessed the effect of N-acetyl-d-glucosamine on sCR1-MBL binding.
  • Examined C1q inhibition of MBL binding to sCR1.
  • Studied MBL binding to polymorphonuclear leukocytes (PMNs) in relation to CR1 expression.

Related Experiment Videos

  • Evaluated CR1's role in erythrocyte adhesion to MBL and phagocytosis of MBL-opsonized bacteria.

    • Main Results:

    • Radioiodinated MBL demonstrated binding to immobilized sCR1 with a dissociation constant of 5 nM.
    • N-acetyl-d-glucosamine did not inhibit MBL binding to sCR1, indicating the carbohydrate-binding site is not involved.
    • C1q inhibited MBL binding to sCR1, suggesting a shared or adjacent binding site.
    • MBL binding to PMNs correlated positively with CR1 expression.
    • CR1 mediated erythrocyte adhesion to MBL and acted as a phagocytic receptor for MBL-opsonized bacteria.

    Conclusions:

    • Complement receptor 1 (CR1) binds to both soluble and cellular Mannan-binding lectin (MBL).
    • CR1 functions as a cellular receptor for MBL.
    • This finding supports the role of CR1 in MBL-mediated biological functions.