Antibody

An antibody (Ab) or immunoglobulin (Ig) is a large, Y-shaped <a href="/facts/Protein/Jxmagu3E">protein</a> belonging to the <a href="/facts/Immunoglobulin_superfamily/Wveu4BIL">immunoglobulin superfamily</a> which is used by the <a href="/facts/Immune_system/HRCTf1pb">immune system</a> to identify and neutralize <a href="/facts/Antigen/9JlAernG">antigens</a> such as <a href="/facts/Pathogenic_bacteria/X5QcVN5j">bacteria</a> and <a href="/facts/Virus/mf88Bcbl">viruses</a>, including those that cause disease. Antibodies can recognize virtually any size antigen, able to perceive diverse chemical compositions. Each antibody recognizes one or more specific <a href="/facts/Antigen/9JlAernG">antigens</a>. Antigen literally means "antibody generator", as it is the presence of an antigen that drives the formation of an antigen-specific antibody. Each tip of the "Y" of an antibody contains a <a href="/facts/Paratope/PnHjQp4j">paratope</a> that specifically binds to one particular <a href="/facts/Epitope/PL0oBuGh">epitope</a> on an antigen, allowing the two molecules to bind together with precision. Using this mechanism, antibodies can effectively "tag" a <a href="/facts/Microbe/pysJYcE2">microbe</a> 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).
More narrowly, an antibody (Ab) can refer to the free (secreted) form of these proteins, as opposed to the membrane-bound form found in a <a href="/facts/B_cell/6Y1tgwwp">B cell</a> receptor. The term immunoglobulin can then refer to both 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 sites at both tips of the antibody come in an equally wide variety. The rest of the antibody structure is much less variable; in humans, antibodies occur in five <a href="/facts/Isotype_(immunology)/5TKdsJLE">classes</a>, sometimes called isotypes: <a href="/facts/IgA/G0HzhnWt">IgA</a>, <a href="/facts/IgD/ASxlMgyy">IgD</a>, <a href="/facts/IgE/76uGAl7k">IgE</a>, <a href="/facts/IgG/cKzc83tk">IgG</a>, and <a href="/facts/IgM/23PjpgIQ">IgM</a>. Human IgG and IgA antibodies are also divided into discrete subclasses (IgG1, IgG2, IgG3, 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 functions and distribution throughout the body may be different. For example, mouse IgG1 is closer to human IgG2 than human IgG1 in terms of its function.
The term <a href="/facts/Humoral_immunity/qG9I4pGf">humoral immunity</a> 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 <a href="/facts/Cell-mediated_immunity/vPX39rt1">cell-mediated immunity</a>, which generally describes the responses of <a href="/facts/T_cell/5z6PQ9UN">T cells</a> (especially cytotoxic T cells). In general, antibodies are considered part of the <a href="/facts/Adaptive_immune_system/bc7zT1Jo">adaptive immune system</a>, though this classification can become complicated. For example, natural IgM, which are made by B-1 lineage 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- they recognize multiple distinct (unrelated) antigens. These can work with the <a href="/facts/Complement_system/vRSrQDUv">complement system</a> in the earliest phases of an immune response to help facilitate clearance of the offending antigen and delivery of the resulting <a href="/facts/Immune_complex/s4kKT3lc">immune complexes</a> to the <a href="/facts/Lymph_node/vkwfcQjH">lymph nodes</a> or <a href="/facts/Spleen/6NKn9d8s">spleen</a> for initiation of an immune response. Hence in this capacity, the function of antibodies is 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 <a href="/facts/Germline/QI4bKK8Q">germline</a>), and are a manifestation of immunological memory.
In the course of an immune response, B cells can progressively <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiate</a> into antibody-secreting cells or into memory B cells. Antibody-secreting cells comprise plasmablasts and <a href="/facts/Plasma_cell/1fY4bFHR">plasma cells</a>, which differ mainly in the degree to which they secrete antibody, their lifespan, metabolic adaptations, and surface markers. Plasmablasts are rapidly proliferating, short-lived cells produced in the early phases of the immune response (classically described as arising extrafollicularly rather than from a <a href="/facts/Germinal_center/hdCfNIQc">germinal center</a>) which have the potential to differentiate further into plasma cells. Occasionally plasmablasts are mis-described as short-lived plasma cells; formally this is incorrect. Plasma cells, in contrast, do not divide (they are <a href="/facts/Terminally_differentiated/bCVqUG7w">terminally differentiated</a>), and rely on survival niches comprising specific cell types and cytokines to persist. Plasma cells will secrete huge quantities of antibody regardless of whether or not their cognate antigen is present, ensuring that antibody levels to the antigen in question do not fall to 0, provided the plasma cell stays alive. The rate of antibody secretion, however, can be regulated, for example, by the presence of adjuvant molecules that stimulate the immune response such as <a href="/facts/Toll-like_receptor/hj4qIWP8">TLR</a> ligands. Long-lived plasma cells can live for potentially the entire lifetime of the organism. Classically, the survival niches that house long-lived plasma cells reside in the bone marrow, though it cannot be assumed that any given plasma cell in the bone marrow will be long-lived. However, other work indicates that survival niches can readily be established within the mucosal tissues- though the classes of antibodies involved show a different hierarchy from those in the bone marrow. B cells can also differentiate into memory B cells which can persist for decades similarly to long-lived plasma cells. These cells can be rapidly recalled in a secondary immune response, undergoing class switching, affinity maturation, and differentiating into antibody-secreting cells.
Antibodies are central to the immune protection elicited by most vaccines and infections (although other components of the immune system certainly participate and for some diseases are considerably more important than antibodies in generating an immune response, e.g. in the case of <a href="/facts/Shingles/2rEq69rr">herpes zoster</a>). Durable protection from infections caused by a given microbe – that is, the ability of the microbe to enter the body and begin to replicate (not necessarily to cause disease) – depends on sustained production of large quantities of antibodies, meaning that effective vaccines ideally elicit persistent high levels of antibody, which relies on long-lived plasma cells. At the same time, many microbes of medical importance have the ability to mutate to escape antibodies elicited by prior infections, and long-lived plasma cells cannot undergo affinity maturation or class switching. This is compensated for through memory B cells: novel variants of a microbe that still retain structural features of previously encountered antigens can elicit memory B cell responses that adapt to those changes. It has been suggested that long-lived plasma cells secrete B cell receptors with higher affinity than those on the surfaces of memory B cells, but findings are not entirely consistent on this point.

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Antibody