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Related Experiment Videos

Identification of complement regulatory domains in human factor H

D L Gordon1, R M Kaufman, T K Blackmore

  • 1Department of Microbiology and Infectious Diseases, Flinders Medical Centre, Australia.

Journal of Immunology (Baltimore, Md. : 1950)
|July 1, 1995
PubMed
Summary

Factor H regulates complement activation using short consensus repeat (SCR) domains. Researchers identified that SCR domains 1-3 are essential for cofactor activity, with SCR 1-4 needed for full function in complement regulation.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Factor H is a key regulator of the complement system, preventing damage to host cells.
  • It comprises 20 short consensus repeat (SCR) domains, crucial for its C3b/C4b-binding and regulatory functions.

Purpose of the Study:

  • To identify the specific short consensus repeat (SCR) domains within Factor H responsible for its complement regulatory cofactor activity.
  • To determine the minimal and optimal SCR units required for Factor H's function in C3b cleavage and cell protection.

Main Methods:

  • Constructing and expressing deletion mutants of Factor H's N-terminal SCR domains (1-5) in Chinese hamster ovary (CHO) cells.
  • Assessing the cofactor activity of secreted Factor H fragments for factor I-mediated C3b cleavage.

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  • Evaluating cell protection against complement-mediated lysis using cells expressing functional Factor H constructs.

    • Main Results:

    • Deletion of SCR 2 or 3 abolished cofactor activity, while SCR 1, 4, and 5 deletions retained partial or full activity.
    • The SCR 1-3 unit was sufficient for cofactor activity, but SCR 1-4 was necessary for full activity.
    • Cells expressing a Factor H SCR 1-5 construct with a GPI anchor were protected against complement-mediated cytotoxicity.

    Conclusions:

    • The N-terminal SCR domains of Factor H, specifically SCRs 1-3, are critical for its cofactor activity in complement regulation.
    • A functional unit of three to four consecutive SCR domains is likely involved in the regulation of C3 convertase by Factor H.
    • These findings delineate the functional domains of Factor H and provide insights into complement system regulation.