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Related Concept Videos

B Cell Activation and Differentiation01:24

B Cell Activation and Differentiation

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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.
When naive B cells encounter a specific antigen that can bind to the B cell receptor (BCR) on their surface, they undergo sensitization to respond to the antigen's presence. Sensitization begins with...
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Special Features of Adaptive Immunity01:20

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The adaptive immune system, a crucial component of the overall immune response, offers a highly specialized defense against pathogens. It involves specific cell types and features, enabling it to combat infections effectively and efficiently.
The primary cell types involved in adaptive immunity are T cells and B cells. Each type has a unique role in defending the body against pathogens. T cells are responsible for cell-mediated immunity. They identify and eliminate infected cells directly,...
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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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Antibody Structure01:10

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Overview
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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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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Commonly used fusion techniques — electroporation,...
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Antibody Structure and Classes01:25

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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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Engineering B cells to Express Fully Customizable Antibodies with Enhanced Fc Functions.

Paula Cannon1, Chun Huang1, Atishay Mathur1

  • 1Department of Molecular Microbiology and Immunology, Keck School of Medicine of the University of Southern California, Los Angeles, California, USA.

Research Square
|September 18, 2025
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Summary
This summary is machine-generated.

Genome editing reprograms B cells to create custom heavy chain only antibodies (HCAbs). This versatile platform allows tailoring antibody function, half-life, and structure for enhanced therapeutic potential.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Biotechnology

Background:

  • B cells naturally produce antibodies crucial for immune response.
  • Antibody engineering aims to enhance therapeutic efficacy and specificity.
  • Current antibody therapies face limitations in effector function and half-life.

Purpose of the Study:

  • To engineer B cells for the production of customized Heavy chain only antibodies (HCAbs).
  • To explore the flexibility of the immunoglobulin Heavy chain locus (IGH) editing platform.
  • To enhance antibody effector functions, extend half-life, and control antibody structure.

Main Methods:

  • Utilized genome editing within the IGH constant region to reprogram B cells.
  • Engineered cells to express both surface B cell receptor (BCR) and secreted HCAb isoforms.
  • Introduced specific mutations to customize the Fc domain, enforce homodimerization, and add C-terminal domains.

Main Results:

  • Successfully reprogrammed B cells to express functional HCAbs with custom recognition domains.
  • Demonstrated the ability to modify the Fc domain for enhanced effector functions and extended half-life.
  • Achieved obligate HCAb homodimerization, preventing unwanted pairing with endogenous antibody chains.
  • Showcased the accommodation and preferential expression of additional C-terminal domains in secreted HCAbs.

Conclusions:

  • The HCAb editing platform offers significant flexibility for creating fully customized antibody molecules.
  • Engineered B cells can be leveraged to produce therapeutic antibodies with tailored properties.
  • This approach provides a powerful tool for advancing antibody-based therapies by harnessing B cell biology.