How Antibodies Defend Your Body (original) (raw)

Immunoglobulin G is the most abundant immunoglobulin. ALFRED PASIEKA/Science Photo Library/Getty Images

Updated on December 04, 2019

Antibodies (also called immunoglobulins) are specialized proteins that travel through the bloodstream and are found in bodily fluids. They are used by the immune system to identify and defend against foreign intruders to the body.

These foreign intruders, or antigens, include any substance or organism that evokes an immune response.

Examples of antigens that cause immune responses include

Antibodies recognize specific antigens by identifying certain areas on the surface of the antigen known as antigenic determinants. Once the specific antigenic determinant is recognized, the antibody will bind to the determinant. The antigen is tagged as an intruder and labeled for destruction by other immune cells. Antibodies protect against substances prior to cell infection.

Production

Antibodies are produced by a type of white blood cell called a B cell (B lymphocyte). B cells develop from stem cells in bone marrow. When B cells become activated due to the presence of a particular antigen, they develop into plasma cells.

Plasma cells create antibodies specific to a certain antigen. Plasma cells generate the antibodies essential to the branch of the immune system known as the humoral immune system. Humoral immunity relies on the circulation of antibodies in bodily fluids and blood serum to identify and counteract antigens.

When an unfamiliar antigen is detected in the body, it can take up to two weeks before plasma cells can generate enough antibodies to counteract the specific antigen. Once the infection is under control, antibody production decreases and a small sample of antibodies remain in circulation. If this particular antigen should appear again, the antibody response will be much quicker and more forceful.

Structure

An antibody or immunoglobulin (Ig) is a Y-shaped molecule. It consists of two short polypeptide chains called light chains and two longer polypeptide chains called heavy chains.

The two light chains are identical to each other and the two heavy chains are identical. At the ends of both the heavy and light chains, in the areas that form the arms of the Y-shaped structure, are regions known as antigen-binding sites.

The antigen-binding site is the area of the antibody that recognizes the specific antigenic determinant and binds to the antigen. Since different antibodies recognize different antigens, antigen-binding sites are different for different antibodies. This area of the molecule is known as the variable region. The stem of the Y-shaped molecule is formed by the longer region of the heavy chains. This region is called the constant region.

Classes of Antibodies

Five primary classes of antibodies exist with each class playing a distinct role in the human immune response. These classes are identified as IgG, IgM, IgA, IgD, and IgE. Immunoglobulin classes differ in the structure of the heavy chains in each molecule.

Immunoglobulins (Ig)

There are also a few subclasses of immunoglobulins in humans. The differences in subclasses are based on small variations in the heavy chain units of antibodies in the same class. The light chains found in immunoglobulins exist in two major forms. These light chain types are identified as kappa and lambda chains.

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