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Antibody Structure01:10

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Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
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Comparing domain interactions within antibody Fabs with kappa and lambda light chains.

Raheleh Toughiri1, Xiufeng Wu1, Diana Ruiz1

  • 1a Eli Lilly and Company, Lilly Biotechnology Center , 10300 Campus Point Drive, San Diego , CA 92130 , USA.

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Human antibody fragments (Fabs) with lambda light chains show weaker domain cooperativity than kappa light chain Fabs. Constant domains may primarily stabilize variable domains by reducing hydrophobic exposure.

Keywords:
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Area of Science:

  • Immunology
  • Biophysics
  • Protein Engineering

Background:

  • Immunoglobulin G (IgG) antibodies are complex proteins crucial for antigen binding.
  • Antibody fragments (Fabs) consist of variable (VH, VL) and constant (CH1, CL) domains.
  • Human Fabs with kappa (κ) light chains are well-studied, but thermodynamic properties of lambda (λ) light chain Fabs are less understood.

Purpose of the Study:

  • To investigate and compare the domain contributions to Fab stability for both κ and λ light chain isotypes.
  • To elucidate the thermodynamic properties and inter-domain cooperativity in human Fabs containing λ light chains.
  • To explore the role of constant domains in stabilizing variable domains and the impact of mismatched domain pairings.

Main Methods:

  • Biophysical characterization of human Fabs with κ and λ light chains.
  • Differential scanning calorimetry (DSC) to assess protein unfolding and stability.
  • Analysis of domain cooperativity in both native and mismatched Fab constructs.
  • Assessment of protein secretion and aggregation properties in mammalian cells.

Main Results:

  • λ light chain-containing Fabs exhibit significantly weaker unfolding cooperativity between constant (CH1/Cλ) and variable (VH/Vλ) domains compared to κ light chain Fabs.
  • Constant domains in both κ and λ Fabs appear to play a key role in stabilizing the variable domain interface by minimizing hydrophobic exposure.
  • Mismatched Fab constructs, despite lower thermodynamic stability, secreted as well-behaved monodisperse proteins, unlike aggregated single-chain Fvs (scFvs).

Conclusions:

  • The reduced domain cooperativity in λ Fabs suggests a potentially different evolutionary optimization compared to κ Fabs.
  • Constant domains are critical for Fab stability, primarily by shielding hydrophobic regions of the variable domains.
  • Engineered Fabs with non-native domain pairings can maintain good secretion and solubility properties, offering potential for therapeutic applications.