Antibodies | Wikipedia audio article
Channel: wikipedia tts
Date: 2019-10-04

This is an audio version of the Wikipedia Article:
https://en.wikipedia.org/wiki/Antibody


00:06:30 1 History
00:11:12 2 Forms
00:12:30 3 Antibody–antigen interactions
00:14:02 4 Isotypes
00:16:24 5 Structure
00:17:38 5.1 Immunoglobulin domains
00:18:36 5.2 Heavy chain
00:20:13 5.3 Light chain
00:21:22 5.4 CDRs, Fv, Fab and Fc regions
00:25:11 6 Function
00:27:44 6.1 Activation of complement
00:28:40 6.2 Activation of effector cells
00:30:24 6.3 Natural antibodies
00:31:40 7 Immunoglobulin diversity
00:32:44 7.1 Domain variability
00:34:19 7.2 V(D)J recombination
00:36:33 7.3 Somatic hypermutation and affinity maturation
00:38:31 7.4 Class switching
00:40:53 7.5 Specificity designations
00:41:42 7.6 Asymmetrical antibodies
00:44:36 8 Medical applications
00:44:46 8.1 Disease diagnosis
00:47:15 8.2 Disease therapy
00:48:12 8.3 Prenatal therapy
00:50:09 9 Research applications
00:54:05 10 Regulations
00:54:15 10.1 Production and testing
00:55:25 10.2 Before clinical trials
00:56:15 10.3 Preclinical studies
00:57:31 11 Structure prediction and computational antibody design
01:00:39 12 Antibody mimetic



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SUMMARY
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An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (similarly, 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 or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essential for its invasion and survival). Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions. The production of antibodies is the main function of the humoral immune system.Antibodies are secreted by B cells of the adaptive immune system, mostly by differentiated B cells called plasma cells. Antibodies can occur in two physical forms, a soluble form that is secreted from the cell to be free in the blood plasma, and a membrane-bound form that is attached to the surface of a B cell and is referred to as the B-cell receptor (BCR). The BCR is found only on the surface of B cells and facilitates the activation of these cells and their subsequent differentiation into either antibody factories called plasma cells or memory B cells that will survive in the body and remember that same antigen so the B cells can respond faster upon future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions to continue to survey for invading microorganisms.
Antibodies are glycoproteins belonging to the immunoglobulin superfamily. They constitute most of the gamma globulin fraction of the blood proteins. They are typically made of basic structural units—each with two large heavy chains and two small light chains. There are several different types of antibody heavy chains that define the five different types of crystallisable fragments (Fc) that may be attache ...