Antibodies
Antibodies (Ab) also known as an immunoglobulin (Ig), are specialized, large Y-shaped proteins produced as part of the body’s immune response to infection. Antibodies are used by the immune system to identify and eliminate disease causing foreign objects from the body such as microbes, viruses, bacteria, fungi or parasites, by directly destroying them or by blocking them from infecting cells.
Antibodies work by recognizing and sticking to specific proteins, such as those found on the surfaces of viruses and bacteria, in a highly specific way. When the body encounters a microbe for the first time, immune cells produce antibodies that specifically recognize proteins associated with that particular microbe.
After recovering from an infection or receiving a vaccine, a small number of these antibody-producing immune cells usually remain in the body as memory cells, providing immunity to future infections with the same bug. Because memory cells and antibodies are already present, next time the body encounters the same microbe, the immune response is much faster and can stop the infection from taking hold.
Antibodies are the search battalion of the immune system’s search-and-destroy system, tasked with finding an enemy and marking it for destruction. They’re released from the cell and they go out and hunt. The antibody recognizes a unique molecule of the pathogen, called an antigen.
When antibodies find their target, they bind to it, which then triggers a cascade of actions that vanquish the invader. Antibodies are part of the adaptive immune system, the arm of the immune system that learns to recognize and eliminate specific pathogens.
Each tip of the “Y” of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe (foreign object) or an infected cell for attack by other parts of the immune system, or can neutralize it directly (for example, by blocking a part of a virus that is essential for its invasion).
To allow the immune system to recognize millions of different antigens, the antigen-binding sites at both tips of the antibody come in an equally wide variety. In contrast, the remainder of the antibody is relatively constant. It only occurs in a few variants, which define the antibody’s class or isotype.
Antibodies, which are also called immunoglobulins (Ig), all have the same basic Y-shape, but there are five variations on this theme called: IgA, IgD, IgE, IgG or IgM. Each variation looks slightly different and plays slightly different roles in the immune system. For instance, immunoglobulin G, or IgG, is just one Y, whereas IgM has five Ys stacked together, and each prong can bind one antigen.
The constant region at the trunk of the antibody includes sites involved in interactions with other components of the immune system. The class hence determines the function triggered by an antibody after binding to an antigen, in addition to some structural features. Antibodies from different classes also differ in where they are released in the body and at what stage of an immune response.
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