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Related Concept Videos

Hybridoma Technology01:31

Hybridoma Technology

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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.
Hybridoma Selection
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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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Antibody Actions

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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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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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Related Experiment Video

Updated: Dec 7, 2025

Generation of Murine Monoclonal Antibodies by Hybridoma Technology
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Taking the Hinge off: An Approach to Effector-Less Monoclonal Antibodies.

Jamie Valeich1, Dan Boyd1, Manu Kanwar1

  • 1Pharmaceutical & Biologics Development, Gilead Sciences, 4010 Ocean Ranch Blvd, Oceanside, CA 92056, USA.

Antibodies (Basel, Switzerland)
|September 26, 2020
PubMed
Summary

Deleting the hinge region of monoclonal antibodies (mAbs) effectively eliminates effector functions by preventing Fc receptor binding. This engineered antibody modality offers a promising approach for therapeutic and diagnostic applications.

Keywords:
Antibody-dependent cellular cytotoxicity (ADCC)Fab arm exchangeFc neonatal receptorFcRnFcγ receptorsFcγRIFcγRIIIIgG1IgG4effector functionhingemAbmonoclonal antibody

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Area of Science:

  • Immunology
  • Biotechnology
  • Protein Engineering

Background:

  • Monoclonal antibodies (mAbs) are crucial therapeutics, but their effector functions can cause adverse effects.
  • Current Fc domain engineering strategies to abrogate effector functions have limitations.

Purpose of the Study:

  • To investigate hinge deletion as an alternative strategy for Fc domain silencing in humanized IgG1 and IgG4 mAbs.
  • To evaluate the impact of hinge deletion on Fc receptor binding, target antigen engagement, and pharmacokinetic properties.

Main Methods:

  • Humanized IgG1 and IgG4 monoclonal antibodies were engineered with hinge region deletion.
  • Binding affinities to activating Fc gamma receptors (FcγRI, FcγRIIIA) and the Fc neonatal receptor (FcRn) were assessed.
  • Fc domain engineering, including CH3 domain modification, was employed to stabilize hinge-deleted IgG4s and recover FcRn binding.
  • Pharmacokinetic properties, such as clearance rates, were evaluated.

Main Results:

  • Hinge deletion in humanized IgG1 and IgG4 mAbs completely abolished binding to activating Fc gamma receptors I and IIIA.
  • Target antigen binding remained intact after hinge deletion.
  • Binding to the Fc neonatal receptor was reduced, but Fc engineering allowed for partial affinity recovery.
  • Engineered CH3 domains stabilized hinge-deleted IgG4s and prevented Fab arm exchange.
  • Hinge-deleted mAbs exhibited faster clearance and a 'pacified' Fc profile.

Conclusions:

  • Hinge deletion is a viable strategy to abrogate Fc effector functions of monoclonal antibodies while preserving antigen binding.
  • The resulting hinge-deleted mAbs possess desirable properties, including reduced Fc receptor interaction and altered pharmacokinetics.
  • This engineered antibody modality presents an appealing option for developing novel therapeutic and diagnostic agents.