IgG subclass specificity to C1q determined by surface plasmon resonance using Protein L capture technique

Area of Science:

• Biochemistry
• Immunology
• Biotechnology

Background:

• Recombinant monoclonal antibodies (mAbs) are key biological therapeutics.
• mAbs mimic endogenous IgG, initiating complement-dependent cytotoxicity (CDC) via C1q binding.
• Traditional ELISA methods for measuring C1q binding have limitations.

Purpose of the Study:

• To establish a robust capture method using surface plasmon resonance (SPR) for quantifying C1q binding affinity to antibodies.
• To demonstrate the utility of the SPR method by assessing IgG subclass specificity for C1q binding.

Main Methods:

• Development of a novel capture method utilizing surface plasmon resonance (SPR).
• Measurement of C1q binding affinity to various antibody formats.
• Analysis of IgG subclass-specific C1q binding.

Main Results:

• A new SPR-based method for measuring C1q-antibody interactions was successfully established.
• The method demonstrated sensitivity in detecting differences in C1q binding across IgG subclasses.
• This SPR approach offers a robust alternative to traditional ELISA for assessing CDC initiation potential.

Conclusions:

• The developed SPR method provides a sensitive and robust platform for characterizing C1q binding to monoclonal antibodies.
• Understanding IgG subclass specificity in C1q binding is crucial for optimizing therapeutic antibody efficacy and safety.
• This technique facilitates the development of next-generation antibody therapeutics with enhanced complement-mediated functions.