Antigen and antibodies




 Antigen

The immune system is the body’s defense against infectious organisms and other invaders. Through a series of steps called the immune response, the immune system attacks of organisms and substance that invade body system and cause disease.

The immune system protects the body system from possibly harmful substances by recognizing and responding to antigens.

 

Antigens are substance (usually proteins) on the surface of cells virus’s fungi or bacteria. Non living substances such as toxins, chemicals drugs and foreign particle (such as splinter) can be also antigens. The immune system recognizes and destroys substance that contains antigens.


An antigen (from antibody generating) or immunogen is a substance that prompts the generation of antibodies and can cause immune responses. In immunology, an antigen is the substance that binds specifically to the respective antibody. Antigens are usually proteins or polysaccharides.



Antibodies

Antibodies (also called immunoglobulins) are specialized proteins that travel thorough the blood stream and are found in bodily fluids. They are utilized 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. Bacteria, viruses, pollen, and incompatible blood cell types are examples of antigens that cause immune responses. 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.. Antibodies protect against substances prior to cell infection




Antibody 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 and the two heavy chains are identical to each other. 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. 



Antibody Classes

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)

  • IgG: These molecules are the most plentiful in circulation. They can cross blood vessels and even the placenta to provide protection to a fetus. The heavy chain type in IgG is a gamma chain.

  • IgM: Of all of the immunoglobulins, these are the most massive. They contain five Y-shaped sections each with two light chains and two heavy chains. Each Y-shaped section is attached to a joining unit called a J chain. IgM molecules play a major role in the primary immune response as the initial respondents to new antigens in the body. The heavy chain type in IgM is a mu chain.

  • IgA: Located mainly in body fluids such as sweat, saliva, and mucus, these antibodies prevent antigens from infecting cells and entering the circulatory system. The heavy chain type in IgA is an alpha chain.

  • IgD: The role of these antibodies in the immune response is currently unknown. IgD molecules are located on the surface membranes of mature B cells. The heavy chain type in IgD is a delta chain.

  • IgE: Found mostly in saliva and mucus, these antibodies are involved in allergic responses to antigens. The heavy chain type in IgE is an epsilon chain.

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 identified as kappa and lambda chains.



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