What are the antibodies and their classes?
Antibodies (also known as immunoglobulins, abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.
Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.
The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
Classes of antibodies
While billions of different variable regions are made, the general structure of antibodies falls into just five classes and this is based upon the type of heavy chain present in the antibody. Immunoglobulin G (IgG) is the most abundant circulating antibody, making up 80% of the total antibodies and 75% of that found in serum. It contains a single antibody protein complex, with two heavy chains and two light chains. IgG is the second type of antibody synthesized in response to an infection and is the only antibody that can pass through the wall of small blood vessels to access antigens present in the extracellular spaces. It is also the only antibody capable of crossing the placenta, where it confers the mother's immunity onto the fetus and newborn. This immunity protects a baby for the first 6-12 months of its life and allows it time for its own immune system to mature. IgG is particularly effective at attacking extracellular viruses and protein toxins and is also capable of activating the classic pathway of the complement cascade. It helps to prevent the systemic spread of infection and facilitates recovery from many infections.
IgM is the largest antibody, with five Y structures being joined by their Fc regions in a circular configuration. A J chain (another polypeptide) links the five antibodies together. IgM is present in serum, making up about 10 % of antibodies in the blood. The presence of its ten antigen reactive sites helps agglutinate or clump antigens (see the explanation of this term in the next section), making it easier for the immune system to eliminate them. IgM is more efficient than IgG at activating the complement pathway. IgM is synthesized by plasma cells early in a primary infection and is very important in slowing or stopping the spread of a pathogen during the initial stages of an illness. IgM is also found on mature B cells in a monovalent form, where it serves as a receptor.
IgA is present in serum, mucus, saliva, tears, sweat and milk. Two subclasses with different heavy chains are made, IgA1 and IgA2. IgA1 is synthesized in the bone marrow and makes up most of the serum IgA. IgA2 is synthesized by B cells present in MALT. The antibodies are synthesized as dimers that are joined by a short J chain polypeptide. As the secreted IgA2 passes through the intestinal epithelium, a second secretory protein attaches. Dimerization and binding of the J and secretory proteins make IgA more resistant to proteases present in the environments that it protects. IgA in breast milk interferes with the colonization of the GI tract by harmful microorganisms in the first few months of life. The mother's IgA in the GI tract of newborns keeps these pathogens at low populations, preventing them from causing serious disease, but still allowing the stimulation of the infant's own immune system. The newborn thus develops its own immunity while being partially protected by the mother. IgA molecules do not activate the classical complement pathway, but may activate the alternative complement pathway.
IgE is a monomeric antibody that accounts for only 0.002 % of the total serum antibodies. Almost all IgE is bound to tissue cells, especially mast cells and eosinophils in various parts of the body. Contact of IgE with antigen leads to release of a set of signal molecules from the mast cells, which effectively recruits various agents of the immune response to fight the infection. IgE and MALT serve to detect penetrating pathogens and amplify the immune response in an area leading to the repulsion of the invader. Antigen reactions with IgE are also responsible for atopic allergic reactions (e.g., hives, asthma, hay fever etc.)
IgD is found on the surface of B-lymphocytes and together with monomeric IgM, serves as antigen receptor for the activation of B cell as described previously. IgD is monovalent