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Related Experiment Videos

Identification of murine complement receptor type 2.

J D Fingeroth1, M A Benedict, D N Levy

  • 1Division of Infectious Diseases, Dana-Farber Cancer Institute, Boston, MA 02115.

Proceedings of the National Academy of Sciences of the United States of America
|January 1, 1989
PubMed
Summary

Researchers identified a murine B-cell surface antigen similar to human complement receptor type 2 (CR2). This antigen binds C3d-coated erythrocytes but not Epstein-Barr virus, suggesting functional differences despite structural similarities.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Biology

Background:

  • The complement receptor type 2 (CR2) plays a crucial role in the human immune system, particularly in B-cell activation and Epstein-Barr virus (EBV) binding.
  • Understanding the homologous structures in other species can provide insights into conserved immune functions and evolutionary pathways.

Purpose of the Study:

  • To identify and characterize a murine homolog of the human CR2.
  • To investigate the functional and structural similarities and differences between human and murine CR2.

Main Methods:

  • Immunoprecipitation using rabbit antiserum against human CR2.
  • Analysis of molecular weight and cellular distribution of the murine antigen.
  • Functional assays involving sheep erythrocytes and Epstein-Barr virus.

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  • Screening of a murine B-cell cDNA library with human CR2 cDNA.
  • Blot hybridization to detect corresponding mRNA.

    • Main Results:

    • A Mr 155,000 murine B-cell surface antigen immunoprecipitated by anti-human CR2 antiserum was identified.
    • The murine antigen shares similarities in molecular weight and distribution with human CR2.
    • Murine CR2-expressing cells bind C3d-coated erythrocytes but not EBV.
    • A partial murine CR2 cDNA clone showed significant sequence identity to human CR2, particularly in the intracytoplasmic region and a CR2 repeat.
    • A 4.7 kb mRNA species for murine CR2 was detected in B-cells but not T-cells.

    Conclusions:

    • A murine homolog of human CR2 exists on B-cells, sharing structural and some functional characteristics.
    • The inability to bind EBV suggests functional divergence in viral interaction despite conserved complement-binding capabilities.
    • The characterized murine CR2 provides a valuable tool for studying complement-mediated immunity and B-cell biology in a murine model.