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Immunoglobulins

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Published in: Biology
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This presentation focuses on the different types of immunoglobulins, also known as antibodies produced by our body\'s immune system, their structure and the functions performed by each.

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  1. IMMUNOGLOBULIN - STRUCTURE, ISOTYPES AND BIOLOGICAL FUNdTION - ELSIRANI. 13-PZOét15
  2. 'ANTIBODY Also known as an immunoglobulin . A large Y-shaped protein produced by B cens that is used by the immune system to idenffy and neuralize foreign objects such as bacteria and viruses. ' Ech åp of the Y" ofan anåbody conü.ins a paratope that is specific for one paråcular epitope on an anågen.
  3. STRUCTURE OF ASTYPICAL ANTiÄODV,— Anåbodies are heavy ( — 150kDa) globular plasma proteins. Severalhnmunodobuh domahsmake up the twÖheawchains and the two chains of an anåbody. The variable par6 of an anåbodyarei6 Vregbns, and the consüntpaztis i6 Creäon. A Opicalanübodyconä.izs the followingpar6: 1. Fab re—on 2 Fcreäon 3. Heawchain with one vuiablé (VB) domain followed by a consüntdomain (CHI), a hinge regon, and two more consünt (CA and C') domains. 4. Light cham with one.ariable (VI) and one consünt (CD domain 5. Anågen bindingsite (paratope) 6. re—ons.
  4. Antigen binding site Variable region of the heavychain Light chain Antigen binding site Variable region of c Disulfide bonds Heavy chain I c c the tight chain Constant regions of heavy and loght chains Antigen Antigenic determinant Antigenic binding site Heavy chain B Light chain Immunoglobulins : A. Structure, B. Antigen binding site
  5. GENERAL BIOLOGICAL FUNCTION OF AN ANTIBODY 1. 2 3. 4. Anåbodies conåibute to immunity in three ways: Prevent pathogens from enåy Såmulate removal of pathogens åüer desåucübn of pathogens by smnulaühg the complement pathway. Acåvaåon of the 'classkürcomplementsystem, Passive immunizaåon from the mother. Lysis of enveloped virus—cles long before the adapåve inmune response is acåvated.
  6. ISOTYPES ' In placental mammals there tare five anåbody isotypes known as 144, IgD, lgE, lgc andigM. They differ in-s their såucture, biolo"cal properåes, fimcübna/ locaåons and ability to deal with different anågens.
  7. Second major anåbody component of body fluid. Presentin saliva, tears, breast milk and mucus of bronchial, urinogenital and digesåve fracts. ' Immunoglobulin A plays a criåcal olein mucosal immunity. Between three and five gams are secreted into the intesånallumen each day.
  8. Fonns Serum 144 vs. secretoryIgA 1. 2. Serum IgA or 1441: Monomer Found in serum - 80070 Mostly made by B-cells deriv@from SecretorvIqA or 1442: Dimer Found in secretions — Product oTB-cells located in mucosal memb IgA2is foundin breast milk, tears and saliva. bone: arrow.
  9. lgA Structure Ser-urn - monotner — Secretions (slgA) • Dimer (IIS) • J chain • Secretory component Secretory Piece J Chain
  10. Structure of Secretory lgG J Chai 3 3 3 Carbohydrates 380 kD J Chain 15 kD Secretrog chain 70 kD & Can not bind complement Secretory Protein epithelial cells
  11. FUNCTIONS OF Efficient binding to surface antigens of pathogens. ' Entrapment of air-borne pathogens entering the respiratory tract ' lgA in breast milk protects th •nfant rom infection.
  12. IgD Makes up about of proteins hi the plasma membranes of mature 'B-lyrnphocytes. ugD is also produced m a secretédfonn thatis found in [very småll amounts*in blood serum. They occurhl membrane:bound/fonn on, 'B-cellslll serve as Bcd receptor* *Binding results in the acåvaåoh ofBcellfor < '*profferaåon and differenåaåoh inho anübodjh producing plasmavcellsö
  13. Stråcture „ of/IgD Secretéds1ÉD 'is produced as a monomeric anåbody with two heavy )chains twb Ig light chains.
  14. • Stillcture Mononler - Tail piece lgD 0 C) Tail Piece
  15. ;FuhcFons of/IgD Acåvaübn ofB-cells Respiratow immune B defenseGtin humans. Rélease ofB€e//homeostaüZ' actors.
  16. 12M 'Produced by B cells -05-10% Ito 'IgM is the largest anåbody in the. human circulatory system. 'Mobr class in primary immune response: The first anåbody to appear in response to iniåal exposure to anågen. 'The spleen is the mobr site of IgM producåon.
  17. Smucture of IgM Ito 'IgM forms polymers where mulåple immunoglobulins are covalently hhked.togeåher with disulfide bonds, mosdy as but arso as a hexamer. &Mhas a molecular mass of approMmate1y 970 kDa (in its penämerfonn). A penämenZ'&Mhas 10 binding sites. Typically, however, IgM cannot bind 10 anågens at the same mne because the large size of most anågens hhders biqüg to nearby sites. The J chain is found in penümeric IgM but not in the hexameric form.
  18. lgM J Chain • Structure Pentamer (19S) — Extra domain (CH4) — J chain
  19. EucdQ2E..QUgM Ito IgM anåbodies appear early'iöthe course of an infecåon. ' DemonsåaühgWanü'bo&s in a paåent'S serum indicates recent lhfecübn, or in a neonate's serum indicates iqåautenhe infecåon (e.g. congenihl rubella). The development of and-donor IgM after organ åansplanüåon is not associated with g•aft r&cübn butitmayhave a protecåve effect Effecåve complement acåvaübn. Agluånaåon of pathogens.
  20. Normal Joint Muscle Bursa Tendon Bone Synovial Membrane Synovial fluid Joint capsule Cartilage Rheumatoid Arthritis Bone erosion Swollen inflamed Synovial Membrane
  21. Rheumatoid arthritis (late stage) BOUtonniere deformity of thumb Ulnar deviation of metacarpophalangeal joints Swan-neck deformity of fingers
  22. I'E is normally present in serum in eyfremely low concenfraåon, which increases in allergicpaåentsø o Most of the IgE is found in the bound form to mast cells basophilse
  23. tCÄSüucture of IgE exists as monomer consisång of tv!' heavy chains (e chain) and two light chains, with the e chain containing 4 Ig-like constant domains (G I-G4)ø
  24. lgE Structure — Monomer — Extra domain (CHO 0 cc4
  25. Jg&ECNCCtQNS ly involved in allergic reactions. also plays an essential role in Ope I hypersensitivity reactions such as hay fever and asi/!lja Degranulation of basophils and mast cells, and release histamine and other mediators of allérgy to give allergic response. IgE also plays a pivotal role in allergic conc@ps, L) such as anaphylactic reactions to certain dru@,) e stings, and antigen preparations us desensitization immunotherapy.
  26. IgG is the most abundant anåbody isotype foundin the circulaåon - IgG molecules are synthesized and secreted by plasma B cells on secondary unmune response. 'J)subclasses of1gG: IgG1 - 9.0mg/mL and1gG4 - 0.4 micro g/mL
  27. ' hnmunog/obuffn C is a protem complex composed of four pepåde chains — Ovo idenåcal heavy chains and two idenåcal light chains arranged a Y-shape typical of anübody monomers. Ech IgG has two sites.
  28. lgG Structure Monomer (7 S) lgG1, lgG2 and lgG4 lgG3
  29. FUNCTIONS OF IgCproæcÜ de body@m infecåon wid exüaællularpåogense IgC acåvaæs de classiælpaåwayofåe complementsysæm. IgG neuüaffzes toüns., andalso opsonisespåogens, IgG also plays an imporünt role in æll- mediaed cytotoMdty64DCC) and inüaællular pmæobsis. IgGig also Type Hand Type m Hypersensiåvity, ' Itis de human placenä, 'Mlong wÆ de breastmilk, residual absorbed de pkænäpmvides de neonaæ wiåhumoral unity before io own immune sysem develops. Colosüum coneins a hi" colosüum ege of
  30. -lgG Heavy chains lgE $ Heavy chains lgA Heavy chains lgD Heavy chains lgM 02 Disulfide bond 11Heavy chain Light 4 chains
  31. 05.5

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