Antibody
An antibody (Ab), or immunoglobulin (Ig), is a large protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as those that exist on bacteria and virus cells, including those that cause disease. Each individual antibody recognizes one or more specific antigens, and antigens (a portmanteau of "antibody generator") of virtually any size and chemical composition can be recognized. Each of the branching chains comprising the "Y" of an antibody contains a paratope (the antigen-binding site) that specifically binds to one particular epitope (a specific part of an antigen bound by the paratope) on an antigen, allowing the two molecules to bind together with precision. Using this mechanism, antibodies can effectively "tag" the antigen (or a microbe or an infected cell bearing such an antigen) for attack by cells of the immune system, or can neutralize it directly (for example, by blocking a part of a virus that is essential for its ability to invade a host cell).
Antibodies may be borne on the surface of an immune cell, as in a B cell receptor, or they may exist freely by being secreted into the extracellular space. The term antibody generally refers to the free (secreted) form, while the term immunoglobulin can refer to either forms. Since they are, broadly speaking, the same protein, the terms are often treated as synonymous.
To allow the immune system to recognize millions of different antigens, the antigen-binding paratopes at each tip of the antibody come in an equally wide variety. The rest of an antibody's structure is much less variable; in humans, antibodies occur in five classes or isotypes: IgA, IgD, IgE, IgG, and IgM. Human IgG and IgA antibodies are also divided into discrete subclasses (IgG1, IgG2, IgG3, and IgG4; IgA1 and IgA2). The class refers to the functions triggered by the antibody (also known as effector functions), in addition to some other structural features. Antibodies from different classes also differ in where they are released in the body and at what stage of an immune response. Between species, while classes and subclasses of antibodies may be shared (at least in name), their function and distribution throughout the body may be different, which complicates the use of animal models in studying antibodies. For example, mouse IgG1 is closer to human IgG2 than to human IgG1 in terms of its function.
The term humoral immunity is often treated as synonymous with the antibody response, describing the function of the immune system that exists in the body's humors (fluids) in the form of soluble proteins, as distinct from cell-mediated immunity, which generally describes the responses of T cells (especially killer T cells). In general, antibodies are considered part of the adaptive immune system, though this classification can become complicated. For example, natural IgM, which are made by B-1 cells that have properties more similar to innate immune cells than adaptive, refers to IgM antibodies made independently of an immune response that demonstrate polyreactivity—i.e. they recognize multiple distinct (unrelated) antigens. These can work with the complement system in the earliest phases of an immune response to help facilitate clearance of the offending antigen and delivery of the resulting immune complexes to the lymph nodes or spleen for initiation of an immune response. Hence in this capacity, the functions of antibodies are more akin to that of innate immunity than adaptive. Nonetheless, in general, antibodies are regarded as part of the adaptive immune system because they demonstrate exceptional specificity (with some exceptions), are produced through genetic rearrangements (rather than being encoded directly in the germline), and are a manifestation of immunological memory.
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