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Cross-reactivity

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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...

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.
Neutralization
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...

Antibody Structure and Classes

Antibody Structure and Classes

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.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.

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Snakes antibodies.

Francisco Gambón-Deza¹, Christian Sánchez-Espinel, Serafín Mirete-Bachiller

¹Servicio Gallego de Salud (SERGAS) Unidad de Inmunología, Hospital do Meixoeiro, Carretera de Madrid s/n, Vigo, Pontevedra, Spain. fgambon@gmail.com

Developmental and Comparative Immunology

|March 20, 2012

Summary

Researchers investigated snake immunoglobulin genes, finding immunoglobulin M, D, and two types of Y (IgYa, IgYb) in all species. A third IgY type (IgYc) was discovered in some snakes, suggesting an evolutionary link to IgYb. Lambda was the only light chain identified.

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Area of Science:

* Comparative genomics
* Immunology
* Evolutionary biology

Background:

* Immunoglobulins (antibodies) are crucial for vertebrate adaptive immunity.
* Previous research characterized immunoglobulins in some reptiles (squamates).
* Snakes (Serpentes) represent a distinct evolutionary lineage within squamates, prompting investigation into their unique immunoglobulin repertoire.

Purpose of the Study:

* To analyze the immunoglobulin coding genes in snakes.
* To understand how evolutionary changes in snakes have impacted their immunoglobulin diversity.
* To identify the types and variations of immunoglobulins present in the suborder Serpentes.

Main Methods:

* Analysis of five snake transcriptomes.
* Examination of two snake genome draft sequences.
* Exhaustive search for immunoglobulin coding sequences and light chains.

Main Results:

* All studied snakes possess genes for immunoglobulin M (IgM), immunoglobulin D (IgD), and two classes of immunoglobulin Y (IgYa and IgYb).
* A novel third class of immunoglobulin Y (IgYc), characterized by a three-domain constant region lacking CH2, was identified in *Thamnophis elegans* and *Python molurus*.
* The lambda light chain was the only type found across all investigated snake species.

Conclusions:

* The findings elucidate the immunoglobulin gene repertoire in snakes, highlighting conserved and novel immunoglobulin classes.
* Evidence suggests that IgYb is the evolutionary precursor to the newly identified IgYc class.
* This study provides a comprehensive overview of snake immunoglobulins, contributing to our understanding of reptilian immune system evolution.