Resources | Subject Notes | Biology
This section explores the molecular structure of antibodies and how this structure dictates their functions in the immune system. We will also examine the principles behind vaccination and how it leverages antibody production for long-term immunity.
Antibodies, also known as immunoglobulins (Ig), are Y-shaped proteins produced by plasma cells in response to an antigen. The structure of an antibody is highly conserved across different classes but exhibits key variations in its functional regions.
An antibody molecule consists of four polypeptide chains: two heavy chains and two light chains. These chains are linked together by disulfide bonds. The antibody structure can be divided into two main regions:
The antigen-binding site within the Fab region is formed by the complementarity-determining regions (CDRs) on the V domains. These CDRs make specific contact with the antigen, leading to a highly specific interaction. The shape of the antigen-binding site is complementary to the shape of the antigen, much like a lock and key.
There are five main classes of antibodies, each with distinct properties and functions:
Antibody Class | Abbreviation | Major Function | Distribution |
---|---|---|---|
IgG | IgG | Most abundant in blood and tissue fluids; provides long-term immunity; crosses the placenta. | Blood, tissue fluids, breast milk |
IgM | IgM | First antibody produced during an infection; effective at complement activation. | Blood |
IgA | IgA | Found in mucosal secretions (e.g., saliva, tears, breast milk); protects mucosal surfaces. | Mucosal surfaces, breast milk |
IgE | IgE | Involved in allergic reactions and parasitic infections. | Bound to mast cells and basophils |
IgD | IgD | Function is not fully understood; found on B cells. | B cells |
Vaccination is a method of preventing infectious diseases by exposing the body to a weakened or inactive form of a pathogen (or a part of it). This triggers an immune response, leading to the production of antibodies against the pathogen. These antibodies provide protection if the individual is later exposed to the live pathogen.
Vaccines can be categorized based on the type of antigen they contain:
The specific structure of an antibody, particularly the amino acid sequence of the CDRs, determines its ability to bind to a specific antigen. The Fc region's structure dictates its interactions with other immune cells, such as macrophages and complement proteins. This intricate relationship between structure and function is crucial for the effectiveness of the antibody response and the success of vaccination.