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Antibody Structure

Antibody Structure

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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...

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Measuring Antibody Orientation at the Bacterial Surface.

Oonagh Shannon¹, Pontus Nordenfelt²

¹Division of Infection Medicine, Department of Clinical Sciences, Lund University, BMC B14, SE-221 84, Lund, Sweden.

Methods in Molecular Biology (Clifton, N.J.)

|December 4, 2016

Summary

This study introduces a new method to detect how bacteria bind antibodies, differentiating between Fc and Fab regions. This technique helps understand bacterial immune evasion strategies and their role in disease.

Keywords:

Bacteria Flow cytometry IdeS IgG IgG-binding proteins

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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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Published on: March 24, 2017

Area of Science:

Microbiology
Immunology
Biochemistry

Background:

Bacteria can evade immune responses by binding to antibodies, altering their orientation to reduce immune signaling.
Antibody orientation on bacterial surfaces is crucial for understanding pathogenesis and host-pathogen interactions.

Purpose of the Study:

To develop and present a novel method for quantifying human immunoglobulin G (IgG) binding orientation on bacterial surfaces.
To distinguish between Fc-mediated and Fab-mediated antibody binding to bacterial pathogens.

Main Methods:

Treatment of antibody-coated bacteria with the bacterial enzyme Immunoglobulin G-degrading enzyme (IdeS) to cleave IgG.
Detection of remaining Fc and Fab fragments using fluorescently labeled Fab antibodies to determine binding proportions.

Main Results:

The described method provides a straightforward and rapid assessment of antibody orientation on bacterial surfaces.
Successfully differentiates between Fc and Fab binding of human IgG to bacteria.

Conclusions:

This technique offers a valuable tool for studying bacterial immune evasion mechanisms involving antibody interactions.
The principle is adaptable for other biological systems requiring differentiation of antibody Fc and Fab binding.