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Antigen-antibody interaction

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778:. It is used for qualitative and quantitative determination of both antigen and antibody. It involves the reaction of soluble antigen with soluble antibodies to form large interlocking aggravated called lattice. It occurs in two distinct stages. Firstly, the antigen and antibody rapidly form antigen-antibody complexes within few seconds and this is followed by a slower reaction in which the antibody-antigen complexes forms lattices that precipitate from the solution. 122: 57:. The antigens and antibodies combine by a process called agglutination. It is the fundamental reaction in the body by which the body is protected from complex foreign molecules, such as pathogens and their chemical toxins. In the blood, the antigens are specifically and with high affinity bound by antibodies to form an antigen-antibody complex. The immune complex is then transported to cellular systems where it can be destroyed or deactivated. 155: 113:
the blood. There are many antibodies and each is specific for a particular type of antigen. Thus immune response in acquired immunity is due to the precise binding of antigens to antibody. Only very small area of the antigens and antibody molecules actually interact through complementary binding sites, called epitopes in antigens and paratopes in antibody.
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Normally antibodies can detect and differentiate molecules from outside of the body and those produced inside the body as a result of cellular activities. Self molecules as ignored by the immune system. However, in certain conditions, the antibodies recognise self molecules as antigens and triggers
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are all known to be involved depending on the interaction sites. Non-covalent bonds between antibody and antigen can also be mediated by interfacial water molecules. Such indirect bonds can contribute to the phenomenon of cross-reactivity, i.e. the recognition of different but related antigens by a
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Immunity developed as an individual is exposed to antigens is called adaptive or acquired immunity, in contrast to immunity developed at birth, which is innate immunity. Acquired immunity depends upon the interaction between antigens and a group of proteins called antibodies produced by B cells of
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The principles of specificity and cross-reactivity of the antigen-antibody interaction are useful in clinical laboratory for diagnostic purposes. One basic application is determination of ABO blood group. It is also used as a molecular technique for infection with different pathogens, such as HIV,
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Structure of hen egg lysozyme (HEL) antigen. (A) The 3-D structure of HEL (CPK representation) together with three Abs (ribbon representation). (B) The structure of HEL colored according to the same three epitopes as in (A). (C) The structure of HEL colored according to the epitopes predicted by
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these are roughly from residues 28 to 35, from 49 to 59, and from 92 to 103, respectively. HV3 is the most variable part. Thus these regions may be part of a paratope, the part of an antibody that recognizes and binds to an antigen. The rest of the V region between the hypervariable regions are
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for that antigen. Since antibodies are bivalent or polyvalent, this is the sum of the strengths of individual antibody-antigen interactions. The strength of an individual interaction between a single binding site on an antibody and its target epitope is termed the affinity of that interaction.
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where, at equilibrium, c is the concentration of free ligand, r represents the ratio of the concentration of bound ligand to total antibody concentration and n is the maximum number of binding sites per antibody molecule (the antibody valence).
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Braden, BC; Dall'Acqua, W; Eisenstein, E; Fields, BA; Goldbaum, FA; Malchiodi, EL; Mariuzza, RA; Schwarz, FP; Ysern, X; Poljak, RJ (1995). "Protein motion and lock and key complementarity in antigen-antibody reactions".
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polypeptide. This region, called the variable (V) domain, is composed of amino acid sequences that define each type of antibody and their binding affinity to an antigen. The combined sequence of variable light chain
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There are several types of antibodies and antigens, and each antibody is capable of binding only to a specific antigen. The specificity of the binding is due to specific chemical constitution of each antibody. The
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Taylor, Charles W.; Chakrabarty, Subhas; Schauder, Keith S.; Yeoman, Lynn C. (1983). "Identification of Cytosolic Antigens from GW-39 Adenocarcinoma Cells by Crossed Immunoelectrophoresis and Immunofluorescence".
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depending on the type of antigens and antibodies involved. Such conditions are always harmful and sometimes deadly. The exact nature of antibody-antigen interaction in autoimmune disease is not yet understood.
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Antigen and antibody interact through a high affinity binding much like lock and key. A dynamic equilibrium exists for the binding. For example, the reaction is a reversible one, and can be expressed as:
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Oda, Masayuki; Uchiyama, Susumu; Noda, Masanori; Nishi, Yoshinori; Koga, Maiko; Mayanagi, Kouta; Robinson, Carol V.; Fukui, Kiichi; Kobayashi, Yuji; Morikawa, Kosuke; Azuma, Takachika (2009).
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It acts on antigen-antibody reaction in which the antibodies cross-link particulate antigens resulting in the visible clumping of the particle. There are two types, namely active and passive
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Lisova, O; Belkadi, L; Bedouelle, Hugues (Apr 2014). "Direct and indirect interactions in the recognition between a cross-neutralizing antibody and the four serotypes of dengue virus".
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Cornaby, Caleb; Gibbons, Lauren; Mayhew, Vera; Sloan, Chad S.; Welling, Andrew; Poole, Brian D. (2015). "B cell epitope spreading: Mechanisms and contribution to autoimmune diseases".
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van Oss, CJ; Good, RJ; Chaudhury, MK (1986). "Nature of the antigen-antibody interaction. Primary and secondary bonds: optimal conditions for association and dissociation".
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Soluble antigens combine with soluble antibodies in presence of an electrolyte at suitable temperature and pH to form insoluble visible complex. This is called a
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Antigen-antibody interaction is used in laboratory techniques for serological test of blood compatibility and various pathogenic infections. The most basic is
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Goldberg, Richard J. (1952). "A Theory of Antibody—Antigen Reactions. I. Theory for Reactions of Multivalent Antigen with Bivalent and Univalent Antibody".
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of the antibody, situated at the variable region of the polypeptide chain. The variable region in turn has hyper-variable regions which are unique
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for the interactions they describe. The lower the dissociation constant, the higher the avidity or affinity, and the stronger the interaction.
1348:"Exploring avidity: understanding the potential gains in functional affinity and target residence time of bivalent and heterobivalent ligands" 1703: 1625: 852: 1054:
Absolom, DR; van Oss, CJ (1986). "The nature of the antigen-antibody bond and the factors affecting its association and dissociation".
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Mian, I.Saira; Bradwell, Arthur R.; Olson, Arthur J. (1991). "Structure, function and properties of antibody binding sites".
1690:, Techniques in Life Science and Biomedicine for the Non-Expert, Cham: Springer International Publishing, pp. 23–30, 563: 1550: 81: 775: 694:{\displaystyle K_{a}={\frac {k_{{\ce {on}}}}{k_{{\ce {off}}}}}={\frac {{\ce {}}}{{\ce { }}}}={\frac {r}{c(n-r)}}} 178: 93: 790: 190: 61: 209: 2025: 743: 1839:"Quantitation of Food Adulterants by Multiple Radial Immunodiffusion. I. Cross-Reacting Antigen Mixtures" 1297:
Estep, Patricia; Reid, Felicia; Nauman, Claire; Liu, Yuqi; Sun, Tingwan; Sun, Joanne; Xu, Yingda (2013).
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The first correct description of the antigen-antibody reaction was given by Richard J. Goldberg at the
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in each antibody. Antigens are bound to antibodies through weak and noncovalent interactions such as
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called framework regions. Each V domain has four framework domains, namely FR1, FR2, FR3, and FR4.
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A special ring test is useful for diagnosis of anthrax and determination of adulteration in food.
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Structural model of an antibody molecule. Rounded portions indicate antigen binding sites.
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Antibodies bind antigens through weak chemical interactions, and bonding is essentially
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in 1952. It came to be known as "Goldberg's theory" (of antigen-antibody reaction).
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The antibody-antigen binding kinetic can be described by the rate equation of a
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is formed from the amino-terminal end of both the light and heavy chains of the
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Janeway, Charles A Jr; Travers, Paul; Walport, Mark; Shlomchik, Mark J (2001).
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The overall strength of the binding of an antibody to an antigen is termed its
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Parry, Christopher M.; Wijedoru, Lalith; Arjyal, Amit; Baker, Stephen (2011).
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are the association and dissociation rate constants, respectively.
751: 153: 120: 1757:"Double-immunodiffusion assay for detecting specific antibodies" 1524:"Immunoglobulins- antigen-antibody reactions and selected tests" 146:) creates three hypervariable regions (HV1, HV2, and HV3). In V 1397:"Binding Revisited-Avidity in Cellular Function and Signaling" 1483:"Assessing human B cell repertoire diversity and convergence" 159:
Discotope (light blue), ellipro (purple), and seppa (pink).
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Thorsen, T.; Klausen, H.; Lie, R. T.; Holmsen, H. (1993).
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Adams, Trudy; Osborn, Sancha; Rijpkema, Sjoerd (2005).
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Sela-Culang, Inbal; Kunik, Vered; Ofran, Yanay (2013).
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unexpected immune responses. This results in different
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Immunobiology: The Immune System in Health and Disease
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Reciprocally, the equilibibrium dissociation constant
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concentration, either in free (,) or bound () state.
212: 913: 693: 551: 419: 293: 1530:. University of South Carolina School of Medicine 1250:"Factors affecting the antigen-antibody reaction" 1162:"Factors affecting the antigen-antibody reaction" 268: 267: 250: 249: 1346:Vauquelin, Georges; Charlton, Steven J. (2013). 793:. They are used in blood tests for diagnosis of 1551:"Antigen/Antibody Tests for Infectious Disease" 1248:Reverberi, Roberto; Reverberi, Lorenzo (2007). 1160:Reverberi, Roberto; Reverberi, Lorenzo (2007). 1481:Imkeller, Katharina; Wardemann, Hedda (2018). 169:Chemical basis of antigen-antibody interaction 37:, is a specific chemical interaction between 8: 1684:"Precipitation and Agglutination Reactions" 1612:. Netherlands: Springer. pp. 309–386. 1254:Blood Transfusion = Trasfusione del Sangue 1166:Blood Transfusion = Trasfusione del Sangue 716:Avidity and affinity can be judged by the 1926: 1854: 1658: 1498: 1422: 1412: 1395:Erlendsson, Simon; Teilum, Kaare (2020). 1371: 1322: 1273: 1185: 968: 958: 920:(5 ed.). 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London: CRC Press. p. 257. 844:Applications of Percolation Theory 322:can therefore be represented as: 25: 564:second-order reversible reaction 72:or epitope is recognized by the 1761:Current Protocols in Immunology 1643:"Immunofluorescence Techniques" 1352:British Journal of Pharmacology 1682:Alhabbab, Rowa Yousef (2018), 685: 673: 654: 648: 643: 637: 630: 624: 542: 536: 529: 523: 518: 512: 410: 404: 399: 393: 386: 380: 286: 280: 270: 245: 235: 229: 221: 215: 1: 1843:Journal of AOAC International 1816:10.1016/j.vaccine.2005.04.017 754:, enzyme-linked immunospot ( 142:) and variable heavy chain (V 31:Antigen-antibody interaction, 1907:Postgraduate Medical Journal 1769:10.1002/0471142735.im0203s00 1726:"Antigen-antibody reactions" 1618:10.1007/978-94-011-1552-0_12 1575:Immunological Investigations 1227:10.1016/j.molimm.2009.09.009 1139:10.1016/0031-6865(94)00046-x 1127:Pharmaceutica Acta Helvetiae 1006:10.1016/0022-2836(91)90617-F 994:Journal of Molecular Biology 1696:10.1007/978-3-319-77694-1_3 1610:Handbook of Immunochemistry 1608:FerenÄŤĂ­k, Miroslav (2013). 1528:Microbiology and Immunology 1460:10.1016/j.imlet.2014.11.001 198:Affinity of the interaction 2047: 1553:. Remedy Health Media, LLC 308:concentration and is the 179:Electrostatic interactions 82:electrostatic interactions 2001:Antigen-antibody reaction 1688:Basic Serological Testing 1587:10.3109/08820138309050753 1414:10.3389/fmolb.2020.615565 1029:Journal of Chromatography 841:Sahimi, Muhammad (1994). 35:antigen-antibody reaction 18:Antigen-antibody reaction 960:10.3389/fimmu.2013.00302 191:hydrophobic interactions 94:hydrophobic interactions 1837:Lietze, Arthur (1969). 1763:. Chapter 2: Unit 2.3. 947:Frontiers in Immunology 62:University of Wisconsin 1856:10.1093/jaoac/52.5.988 785:Agglutination reaction 776:precipitation reaction 770:Precipitation reaction 695: 553: 421: 295: 160: 126: 1919:10.1136/pmj.76.892.80 1755:Hornbeck, P. (2001). 1487:Immunological Reviews 764:immunoelectrophoresis 718:dissociation constant 696: 554: 422: 296: 157: 124: 70:antigenic determinant 1724:Virella, G. (1993). 1660:10.1038/jid.2012.455 1266:10.2450/2007.0047-07 1215:Molecular Immunology 1178:10.2450/2007.0047-07 573: 461: 329: 210: 187:van der Waals forces 129:In an antibody, the 90:Van der Waals forces 78:amino acid sequences 868:Spiers, JA (1958). 828:10.1021/ja01142a045 731:autoimmune diseases 256: 1448:Immunology Letters 1315:10.4161/mabs.23049 760:immunofluorescence 724:Autoimmune disease 691: 549: 417: 291: 275: 161: 127: 117:Antibody structure 1968:10.1586/eri.11.47 1810:(36): 4517–4520. 1730:Immunology Series 1705:978-3-319-77693-4 1627:978-94-010-4678-7 1500:10.1111/imr.12670 1364:10.1111/bph.12106 854:978-0-203-22153-2 822:(22): 5715–5725. 748:blood transfusion 689: 659: 653: 642: 629: 615: 611: 599: 547: 541: 528: 517: 503: 499: 487: 415: 409: 398: 385: 371: 367: 355: 285: 277: 234: 220: 194:single antibody. 47:white blood cells 16:(Redirected from 2038: 2006:Discover Biotech 1988: 1987: 1947: 1941: 1940: 1930: 1898: 1892: 1891: 1867: 1861: 1860: 1858: 1834: 1828: 1827: 1795: 1789: 1788: 1752: 1746: 1745: 1721: 1715: 1714: 1713: 1712: 1679: 1673: 1672: 1662: 1638: 1632: 1631: 1605: 1599: 1598: 1569: 1563: 1562: 1560: 1558: 1546: 1540: 1539: 1537: 1535: 1519: 1513: 1512: 1502: 1478: 1472: 1471: 1443: 1437: 1436: 1426: 1416: 1392: 1386: 1385: 1375: 1358:(8): 1771–1785. 1343: 1337: 1336: 1326: 1294: 1288: 1287: 1277: 1245: 1239: 1238: 1221:(2–3): 357–364. 1206: 1200: 1199: 1189: 1157: 1151: 1150: 1121: 1115: 1114: 1095:10.1002/jmr.2352 1083:J. 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Index

Antigen-antibody reaction
antibodies
B cells
white blood cells
antigens
immune reaction
University of Wisconsin
antigenic determinant
paratope
amino acid sequences
electrostatic interactions
hydrogen bonds
Van der Waals forces
hydrophobic interactions
helminth

Fab (fragment, antigen-binding) region
immunoglobulin

non-covalent
Electrostatic interactions
hydrogen bonds
van der Waals forces
hydrophobic interactions
antibody
antigen
second-order reversible reaction
avidity
dissociation constant
autoimmune diseases

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