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Antibody Actions

Antibody Actions

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 Structure

Antibody Structure

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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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Related Experiment Video

Updated: Jul 16, 2026

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments

Published on: October 15, 2016

Antibody internalization studied using a novel IgG binding toxin fusion.

Yariv Mazor¹, Itay Barnea, Iafa Keydar

¹Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Green Building, Room 202, Tel-Aviv University, Ramat Aviv 69978, Israel.

Journal of Immunological Methods

|March 6, 2007

Summary

This study introduces ZZ-PE38, a novel fusion protein for evaluating antibody-drug conjugates. It effectively targets tumor cells, demonstrating a new method for assessing immunotherapeutic potential based on antibody internalization.

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Area of Science:

Oncology
Immunology
Biochemistry

Background:

Targeted cancer therapies utilize direct and indirect strategies, including monoclonal antibodies and small-molecule drugs.
Indirect approaches involve antibody-drug conjugates or fusion proteins that require antibody internalization into tumor cells for efficacy.
Assessing the internalization potential of antibodies and their target antigens is crucial for developing effective immunotherapeutics.

Purpose of the Study:

To introduce a novel tool, ZZ-PE38, for evaluating the internalization efficiency of antibodies targeting tumor cells.
To demonstrate the specific cytotoxicity of immunocomplexes formed by ZZ-PE38 and tumor-binding IgGs.
To establish a method for assessing the suitability of antibody-antigen pairs for internalization-dependent immunotherapies.

Main Methods:

Development of a novel IgG-binding toxin fusion protein (ZZ-PE38) by linking a ZZ domain to a truncated Pseudomonas exotoxin A.
Formation of complexes between ZZ-PE38 and IgGs that specifically bind to tumor cells.
Assessment of the specific cytotoxicity of these immunocomplexes against target tumor cells.

Main Results:

The study successfully prepared complexes between ZZ-PE38 and tumor-binding IgGs.
These immunocomplexes demonstrated specific cytotoxicity against target tumor cells, confirming effective drug delivery.
The results validate ZZ-PE38 as a tool for evaluating antibody internalization and therapeutic potential.

Conclusions:

ZZ-PE38 is a valuable tool for assessing the internalization capacity of antibodies and their cognate antigens.
This method aids in evaluating the potential of antibodies for use in immunotherapeutics requiring cellular internalization.
The findings support the development of novel antibody-based therapies for cancer treatment.