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Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
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Monoclonal Antibodies Follow Distinct Aggregation Pathways During Production-Relevant Acidic Incubation and

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Therapeutic monoclonal antibody (mAb) aggregation differs by subclass during low pH treatment. IgG1 remains stable, while IgG2 and IgG4 show distinct reversible and irreversible aggregation pathways, impacting biopharmaceutical manufacturing.

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Area of Science:

  • Biopharmaceutical Manufacturing
  • Protein Chemistry
  • Antibody Engineering

Background:

  • Monoclonal antibodies (mAbs) are crucial therapeutics.
  • Aggregation of mAbs is a significant concern in the pharmaceutical industry.
  • Low pH treatment is common in mAb purification and viral inactivation, necessitating understanding of acid-induced aggregation.

Purpose of the Study:

  • To investigate the mechanisms of acid-induced aggregation in different therapeutic monoclonal antibody (mAb) subclasses.
  • To characterize the oligomerization kinetics and reversibility of IgG1, IgG2, and IgG4 mAbs at low pH.
  • To identify subclass-specific aggregation pathways.

Main Methods:

  • Studied three model mAbs (IgG1, IgG2, IgG4) with identical variable regions.
  • Analyzed oligomerization kinetics at pH 3.3 and reversibility upon neutralization.
  • Employed size-exclusion high-performance liquid chromatography (SE-HPLC), small-angle X-ray scattering (SAXS), and dynamic light scattering (DLS).
  • Utilized crystal structure-based spatial aggregation propensity (SAP) calculations.

Main Results:

  • Distinct behaviors observed: IgG1 remained monomeric at acidic pH.
  • IgG2 and IgG4 exhibited two-phase oligomerization processes.
  • IgG2 oligomers partially reverted to monomeric state after neutralization; IgG4 oligomers aggregated irreversibly.
  • Identified subclass-specific aggregation-prone motifs on Fc fragments.

Conclusions:

  • Subtle sequence variations in mAbs significantly influence their response to low pH and neutralization.
  • Orthogonal biophysical methods can differentiate between reversible and irreversible mAb aggregation pathways.
  • Understanding these pathways is critical for optimizing mAb purification and formulation.