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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 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 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.

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Formation of Lipopolysaccharides

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...

Globular Proteins

Globular Proteins

In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...

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Related Experiment Video

Updated: May 24, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β₂-Microglobulin

Published on: March 10, 2021

Echinococcus granulosus antigen B structure: subunit composition and oligomeric states.

Karina M Monteiro¹, Mateus B Cardoso, Cristian Follmer

¹Laboratório de Biologia Molecular de Cestódeos and Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul, Porto Alegre, Rio Grande do Sul, Brazil.

Plos Neglected Tropical Diseases

|March 14, 2012

Summary

Echinococcus granulosus Antigen B (AgB) oligomers are composed of distinct subunits with varying abundances and structural properties. This study reveals new insights into AgB structure, aiding understanding of parasite adaptation during infection.

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

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Published on: October 15, 2019

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Last Updated: May 24, 2026

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β₂-Microglobulin

Published on: March 10, 2021

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

Published on: October 15, 2019

Area of Science:

Parasitology
Structural Biology
Biochemistry

Background:

Antigen B (AgB) is a key secreted protein from Echinococcus granulosus metacestodes.
AgB plays a crucial role in host-parasite interactions during infection.
Understanding AgB's subunit composition and oligomeric states is vital for elucidating its functions.

Purpose of the Study:

To determine the subunit composition of Echinococcus granulosus AgB oligomers.
To investigate the oligomeric states and structural properties of AgB and its recombinant subunits.
To analyze variations in AgB subunit composition and abundance in different cyst origins.

Main Methods:

Mass spectrometry and electrophoretic analysis were used to identify AgB subunits.
Relative subunit abundance was estimated using the exponentially modified protein abundance index (emPAI).
Native PAGE, light scattering, and microscopy characterized oligomeric states; pressure-induced dissociation assessed stability.

Main Results:

AgB8/1, AgB8/2, AgB8/3, and AgB8/4 subunits were identified in both bovine and human cysts.
The AgB8/1 subunit was consistently overrepresented; AgB8/3 abundance varied between host origins.
Recombinant subunits displayed distinct oligomerization behaviors, with rAgB8/3 forming the largest oligomers and exhibiting higher stability.

Conclusions:

This is the first analysis of AgB subunit composition from single hydatid cysts, revealing sample-specific differences.
AgB oligomers are heterogeneous, composed of subunits with unique abundances and oligomerization capabilities.
Findings advance knowledge of AgB structure and expression, offering insights into parasite adaptive strategies in chronic infections.