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Affinity and Avidity01:41

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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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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
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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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Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
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The adaptive immune response, a sophisticated defense mechanism, relies on the activation and differentiation of B lymphocytes, or B cells. These processes enable our bodies to mount a tailored response against specific pathogens such as bacteria, free virus particles, toxins, and parasites.
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Generation of Discriminative Human Monoclonal Antibodies from Rare Antigen-specific B Cells Circulating in Blood
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Affinity Maturation Enhances Antibody Specificity but Compromises Conformational Stability.

Laila Shehata1, Daniel P Maurer1, Anna Z Wec1

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Human monoclonal antibodies (mAbs) from memory B cells and long-lived plasma cells show improved developability. Affinity maturation via somatic hypermutation enhances biophysical properties for therapeutic antibody engineering.

Keywords:
B cellsconformational stabilitydevelopabilityhydrophobicitymonoclonal antibodiespolyreactivity

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Area of Science:

  • Biochemistry
  • Immunology
  • Biotechnology

Background:

  • Monoclonal antibodies (mAbs) are key biotherapeutics.
  • B cell-derived mAbs may possess inherent favorable biophysical properties due to natural selection.
  • Understanding these properties is crucial for therapeutic development.

Purpose of the Study:

  • To evaluate biophysical properties of human mAbs derived from different B cell populations.
  • To investigate the impact of somatic hypermutation (SHM) on mAb developability.
  • To assess the therapeutic potential of B cell-derived mAbs.

Main Methods:

  • High-throughput screening assays were used to assess 400 human mAbs.
  • Evaluated properties included polyreactivity, hydrophobicity, and thermal stability.
  • Correlations between B cell origin, SHM, and biophysical properties were analyzed.

Main Results:

  • mAbs from memory B cells and long-lived plasma cells (LLPCs) exhibited lower polyreactivity, hydrophobicity, and thermal instability compared to naive B cell mAbs.
  • Somatic hypermutation (SHM) showed an inverse correlation with polyreactivity, hydrophobicity, thermal stability, and B cell receptor (BCR) expression.
  • The developability profiles of human B cell-derived mAbs were comparable to clinical mAbs.

Conclusions:

  • B cell differentiation and affinity maturation significantly influence mAb biophysical properties.
  • mAbs derived from memory B cells and LLPCs possess favorable developability characteristics.
  • These findings support the therapeutic potential of B cell-derived mAbs and inform antibody engineering strategies.