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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 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.

Diversity of Antigen Receptors

Diversity of Antigen Receptors

Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...

Cross-reactivity

Cross-reactivity

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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

The complementarity-determining region sequences in IgY antivenom hypervariable regions.

David Gitirana da Rocha¹, Jorge Hernandez Fernandez², Claudia Maria Costa de Almeida³

¹Laboratório de Biologia do Reconhecer (LBR), Centro de Biociências e Biotecnologia (CBB), Universidade Estadual do Norte Fluminense Darcy Ribeiro (UENF), Alberto Lamego Avenue, 2000 - Campos dos Goytacazes, Postal Code 28013-602 Rio de Janeiro, Brazil.

|July 28, 2017

Summary

Researchers developed IgY antibodies from immunized hens to neutralize snake venom toxins. This study details the antibody sequences and their 3D structure for potential antivenom development.

Keywords:

Modeling of biomolecules PCR Sequencing

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Immunoglobulin Gene Sequence Analysis In Chronic Lymphocytic Leukemia: From Patient Material To Sequence Interpretation

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Published on: November 26, 2018

Area of Science:

Immunology
Biochemistry
Molecular Biology

Background:

Snakebite envenoming is a significant global health issue requiring effective antivenoms.
Existing antivenoms often face challenges with specificity, efficacy, and adverse reactions.
Immunoglobulin Y (IgY) antibodies offer a potential alternative for antivenom development.

Purpose of the Study:

To develop and characterize IgY antibodies with high neutralizing activity against snake venom toxins.
To identify and analyze the complementarity-determining region (CDR) sequences of potent anti-snake venom IgY antibodies.
To construct a three-dimensional model of the antibody paratope for structural insights.

Main Methods:

Hens were immunized with *Bitis arietans* (Ba) and *Crotalus durissus terrificus* (Cdt) venoms.
B lymphocytes were isolated to obtain DNA for IgY antibody VLF1, CDR1, CDR2, VLR1, and CDR3 sequences.
Sequences were validated using BLASTp, and registered in gene databases.
Molecular modeling was employed to construct the three-dimensional structure of the IgY single-chain variable fragment (scFv) paratope.

Main Results:

High specificity, affinity, and potent neutralizing antibody titers against Ba and Cdt venoms were achieved.
Specific IgY V_L and V_H sequences against Ba and Cdt venoms were identified and registered (GU815099, GU815098).
The three-dimensional structure of the IgY scFv anti-Ba paratope was successfully constructed using the identified CDR sequences.

Conclusions:

The study successfully developed IgY antibodies with significant venom-neutralizing capabilities.
The characterized antibody sequences and structural models provide a foundation for novel antivenom design.
This research highlights the potential of IgY antibodies as a viable alternative for snakebite treatment.