Antibody Structure Antibody Function Antibodies In The Humoral

An antibody is a protein complex used by the immune system to identify and neutralize foreign objects like bacteria and viruses. Each antibody recognizes a specific antigen unique to its target.

1 Antibody structure

Antibodies are glycoproteins found in the blood and tissue fluids, and are structurally referred to as immunoglobulins. They are synthesized and secreted by B cells of the immune system, which are activated upon binding to substances in the body that are recognized as foreign antigens. The forked end of the "Y" shaped antibody is known as the variable binding domain and stem the constant binding domain. Antibodies stick to pathogens by binding at the variable binding domain and work, in a variety of ways, to help eliminate the antigen that elicited their production, such as by facilitating co-binding to the constant domain by the body's other immune cells. Some of the ways are independent to a particular class of immunoglobulins.

Immunoglobulins are grouped into five classes or isotypes: IgG, IgA, IgM, IgD, and IgE. Differences in the heavy chain constant domains of the immunoglobulin determine its function and which of the following five classes it belongs to. Other immune cells partner with antibodies to eliminate pathogens depending on which IgG, IgA, IgM, IgD, and IgE constant binding domain receptors it can express on its surface.

Immunoglobulins are heavy plasma proteins, often with added sugar chains (see glycosylation) on N-terminal (all antibodies) and occasionally O-terminal (IgA1 and IgD) aminoacid residues. A crude estimation of immunoglobulin levels can be made by protein electrophoresis. Here the plasma proteins are separated into albumin, alpha-globulin s (1 and 2), beta-globulin s (1 and 2) and gamma-globulin s according to weight. Immunoglobulins are all in the gamma region. In some disease states ( myeloma) a very high concentration of one particular protein will show up as a monoclonal band.

To protect itself from any possible antigen, the immune system produces millions of antibody epitopes, each differing in the variable portion that detects and attaches to an antigen. If each type of antibody required a seperate gene to achieve this diversity, the immune system would require many more genes than exist in the genome. Instead, as Susumu Tonegawa showed in 1976, portions of the genome in B lymphocytes can recombine to form all the variation seen in the antibodies. Tonegawa won the Nobel Prize in Physiology or MedicineList of Nobel Prize laureates in Physiology or Medicine from 1901 to the present day. 1900s 1910s 1920s 1930s 1940s 1950s 1960s 1970s 1980s 1990s 2000s 1900s 1910s 1920s 1930s 1940s 1950s 1960s 1970s 1980s 1990s 2000s External links http://www. se/medicin in 1987 for his discovery.

2 Antibody function

2.1 Antibodies in the humoral immune response

Antibodies that recognize viruses can block these directly by their sheer size. The virus will be unable to dock to a cell and infect it, hindered by the antibody. Antibodies that recognize bacteria mark them for ingestion by macrophages. Together with the plasmaBlood plasma is a component of blood. It is the liquid in which blood cells are suspended. Blood plasma contains proteins, nutrients, metabolic end products, hormones, and inorganic electrolytes. Serum is the same as blood plasma except that clotting fact component complementThe complement system is a complex biochemical cascade of the immune system, leading to cytolysis, chemotaxis, opsonization and inflammation, it can mark pathogens for phagocytosis. It consists of more than 35 proteins. 12 which are directly involved in t, antibodies can kill bacteria directly.

The way that antibodies work is by binding with the specific antigen for which the antibody is "designed". This formation of the antigen-antibody results in the stimulation of phagocytosisIn phagocytosis (literally, "cell eating"), large particles are enveloped by the cell membrane of a (usually larger) cell and internalized to form a food vacuole. In animals, phagocytosis is performed by specialized phagocytotic cells or phagocytes, which which is a procedure that cells engulf and destroy particles. An example of an antigen the can do this process is IgG antibodies that prevents the toxin harming the cell by sticking to the cell to destroy it. Antibodies are less effective if they are in low concentrations meaning that it's sometimes less effective in taking care of an already established infection such as viral infections. A viral infection can hide from an antibody so that it does not destroy it when it enters the cell but with bacterial infections they can be destroyed because they are outside of the cell.

Antibodies are effective in preventing any foreign antigens that go into the body. If an antibody can't take care of an already existing infection then it could be very effective in preventing an infection that is about to begin its process in targeting the cells.

2.2 Antibodies in the cell-mediated immune response

When a macrophageMacrophages are part of the immune system. They are circulating scavengers. They are more highly concentrated in the blood, liver, lymph nodes and the spleen), although they are found in all tissues, especially at sites of inflammation. While circulating ingests a pathogenA pathogen is a biological agent that can cause disease to its host. A synonym of pathogen is " infectious agent". The term "pathogen" is most often used for agents that disrupt the normal physiology of a multicellular animal or plant. However, pathogens, it attaches parts of its proteins to a class II MHCThe major histocompatibility complex MHC is a large genomic region or gene family found in most vertebrates containing many genes with important immune system roles. In humans, the MHC spans almost 4 megabases of chromosome 6 and includes more than 200 kn protein. This complex is moved to the outside of the cell membrane, where it can be recognized by a T lymphocyte, which compares it to similar structures on the cell membrane of a B lymphocyte. If it finds a matching pair, the T lymphocyte activates the B lymphocyte, which starts producing antibodies. A B lymphocyte can only produce antibodies against the structure it presents on its surface.

3 Medical applications

"Designed" monoclonal antibody therapy is already being employed in a number of diseases (including rheumatoid arthritis) and is a potential weapon against cancer.

4 Applications in biochemistry

In biochemistry, antibodies are used for immunological identification of proteins, using the Western blot method. A similar technique is used in ELISPOT and ELISA assays, in which detection antibodies are used to detect cell secretions such as cytokines or antibodies.

Antibodies are also used to separate proteins (and anything bound to them) from the other molecules in a cell lysate. These purified antibodies are often produced by injecting the antigen into a small mammal, such as a mouse or rabbit. Blood isolated from these animals contains polyclonal antibodies -- multiple antibodies that stick to the same antigen. If the lymphocytes that produce the antibodies can be isolated and immortalized, then a monoclonal antibody can be obtained. Monoclonal antibodies have much greater specificity than polyclonal antibodies.

5 See also

6 References

Rhoades, Rodney and Richard Pflanzer. Human Physiology, Brooks/Cole, 4th edition

7 External links

Immune system

Humoral immune system - Cellular immune system - Lymphatic system White blood cells - B cells - Antibodies - Antigen ( MHC) Lymphocytes: T cells ( Cytotoxic & Helper) - B cells ( Plasma cells & Memory B cells)

Immune system Immunology Glycoproteins

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