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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...
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Methods for Quantitative Detection of Antibody-induced Complement Activation on Red Blood Cells
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Engineering IgG1 Fc Domains That Activate the Complement System.

Chang-Han Lee1, George Delidakis2

  • 1Department of Biomedical Sciences, Seoul National University College of Medicine, Seoul, South Korea. chlee-antibody@snu.ac.kr.

Methods in Molecular Biology (Clifton, N.J.)
|December 6, 2021
PubMed
Summary
This summary is machine-generated.

Researchers engineered therapeutic IgG antibodies to enhance the clearance of diseased cells. This novel approach focuses on activating the complement pathway while minimizing Fc receptor binding, improving antibody efficacy.

Keywords:
Aglycosylated Fc domainAntibody engineeringBacterial surface displayComplementFc engineering

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Area of Science:

  • Immunology
  • Biotechnology
  • Antibody Engineering

Background:

  • Therapeutic IgG antibodies clear pathologic cells via Fc receptor (FcγR) binding and complement activation.
  • FcγR binding mediates antibody-dependent cellular cytotoxicity (ADCC) and phagocytosis (ADCP).
  • Complement activation leads to complement-dependent cytotoxicity (CDC) and opsonization, enhancing effector cell functions (CDCC, CDCP).

Purpose of the Study:

  • To engineer IgG1 Fc domains with high affinity for C1q (complement initiator) but minimal binding to FcγRs.
  • To develop a method for isolating Fc variants that selectively activate the complement pathway for therapeutic benefit.

Main Methods:

  • Engineered IgG1 Fc domains by introducing mutations.
  • Utilized IgG display in E. coli, lacking glycosylation machinery, to screen large libraries (>2x10^9) of mutated Fc domains.
  • Screened for Fc variants with high C1q binding and low FcγR binding.

Main Results:

  • Successfully engineered IgG1 Fc domains with high C1q binding and reduced FcγR binding.
  • Developed a method for isolating these specific Fc variants.

Conclusions:

  • The engineered Fc domains offer a novel strategy to enhance therapeutic antibody efficacy by selectively engaging the complement pathway.
  • This approach provides a tool to dissect and optimize Fc-mediated effector functions in antibody therapeutics.