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Updated: Jun 17, 2026
06:15
Characterization of Thymus-dependent and Thymus-independent Immunoglobulin Isotype Responses in Mice Using Enzyme-linked Immunosorbent Assay
Published on: September 7, 2018
Recognition of additional roles for immunoglobulin domains in immune function
John P Cannon1, Larry J Dishaw, Robert N Haire
1University of South Florida, Department of Pediatrics, USF/ACH Children's Research Institute, 140 Seventh Avenue South, St. Petersburg, FL 33701, USA. jcannon@health.usf.edu
Seminars in Immunology
|December 17, 2009
Summary
Investigating immune receptors across diverse species reveals the broad functions of immunoglobulin (Ig) domains in host defense. Evolutionary studies highlight common and unique adaptations in immune receptor gene families for fighting infections.
Area of Science:
- Comparative immunology
- Evolutionary biology
- Molecular genetics
Background:
- Immune receptors are crucial for host defense against pathogens.
- Understanding immune receptor evolution provides insight into host-pathogen interactions.
- Immunoglobulin (Ig) domains are key components of many immune receptors.
Purpose of the Study:
- To characterize immune receptors across phylogenetically diverse species.
- To elucidate the evolutionary acquisition of immune function.
- To investigate the roles of variable- and intermediate-type Ig domains.
Main Methods:
- Genetic analysis of immune receptor genes.
- Structural analysis of immune receptor domains.
- Functional studies of immune receptor ligand recognition.
Main Results:
- Immune receptor characterization across disparate species revealed conserved and novel immune functions.
- Variable- and intermediate-type Ig domains exhibit broader roles in ligand recognition than previously known.
- Multigene family diversification and unique adaptations were identified in immune receptor evolution.
Conclusions:
- The study provides unique insights into the evolutionary processes shaping immune receptor diversity and function.
- Understanding Ig domain roles is critical for comprehending host responses to infectious challenges.
- Comparative analysis of immune receptors offers a framework for studying host-pathogen interactions.
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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.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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 consist of four polypeptide chains: two identical heavy...
01:10Antibody 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.
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Antibodies consist of four polypeptide chains: two identical heavy...
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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Neutralization
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Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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01:28Diversity of Antigen Receptors
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