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Related Experiment Videos

On the interaction of the first complement component C1 and its subunit C1q with solid-phase IgM immune complexes.

E M Weiner1

  • 1Department of Medical Microbiology, Medical Faculty, Rheinisch Westfaelische TH, Aachen, FRG.

Scandinavian Journal of Immunology
|October 1, 1988
PubMed
Summary

Solid-phase IgM binds C1q when activated by dextran, with binding strength dependent on antigen concentration. The C1 complex

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Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Immunoglobulin M (IgM) is a crucial component of the innate immune system.
  • The complement system, initiated by C1 complex binding to IgM, plays a vital role in immune responses.

Purpose of the Study:

  • To investigate the interaction between C1 complex, C1q, and solid-phase anti-dextran IgM.
  • To elucidate the conformational changes in IgM upon ligand binding and their effect on C1q fixation.

Main Methods:

  • Enzyme-linked immunosorbent assay (ELISA) was employed to quantify C1q binding to immobilized IgM.
  • The study utilized dextran (B 1355/S) as a specific polyvalent ligand to activate IgM.

Main Results:

  • Immobilized IgM adopts a functional 'staple' conformation upon binding dextran, facilitating C1q fixation.

Related Experiment Videos

  • C1q binding to IgM is antigen-concentration-dependent, with an estimated binding constant (K) of approximately 10(9) M-1.
  • The C1 complex, including C1r2S2, exhibits distinct C1q fixation and dissociation properties compared to free C1q, suggesting altered molecular flexibility.

    • Conclusions:

    • Dextran-induced conformational changes in IgM are essential for C1q recognition and stable binding.
    • The pentameric structure of IgM and the composition of the C1 complex influence the association dynamics of C1q.
    • Altered flexibility of C1q within the C1 complex likely explains the differential binding characteristics observed.