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Post-translationally modified proteins bind and activate complement with implications for cellular uptake and

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The complement system directly binds to certain post-translational modifications (PTMs) like carbamylation and acetylation, enhancing phagocytosis and potentially driving autoimmune responses in rheumatoid arthritis.

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Area of Science:

  • Immunology
  • Biochemistry
  • Rheumatology

Background:

  • Autoimmune diseases like rheumatoid arthritis (RA) involve autoantibodies targeting self-proteins with post-translational modifications (PTMs).
  • The complement system plays roles in immune defense, debris clearance, and antibody response induction.
  • This study investigated the direct interaction between complement and PTMs.

Purpose of the Study:

  • To determine if complement proteins bind directly to various PTMs.
  • To assess the impact of complement activation on PTM-modified proteins.
  • To explore the link between complement genetics and anti-PTM autoimmunity in RA.

Main Methods:

  • Investigated six PTMs: nitration, citrullination, carbamylation, acetylation, MAA, and AGE.
  • Utilized mass spectrometry and plate-bound assays for protein binding analysis.
  • Conducted phagocytosis assays and analyzed complement single nucleotide polymorphisms (SNPs) in RA patients.

Main Results:

  • Complement strongly bound to carbamylation (Ca), acetylation (Ac), MAA, and AGE, but not nitration or citrullination.
  • Ca-, MAA-, and AGE-modified proteins activated the classical complement pathway independently of antibodies.
  • Ac activated the lectin pathway via ficolin-3; complement activation enhanced phagocytosis of modified proteins.

Conclusions:

  • Proteins with Ca, Ac, MAA, or AGE modifications activate complement.
  • Complement opsonization of these PTMs enhances phagocytosis.
  • This interaction may contribute to the development of anti-PTM antibodies in autoimmune diseases.