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64430
Immunoglobulins
Descripción
(Immunology) Mapa Mental sobre Immunoglobulins, creado por w.tetteh el 01/05/2013.
Sin etiquetas
immunology
immunology
Mapa Mental por
w.tetteh
, actualizado hace más de 1 año
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Creado por
w.tetteh
hace más de 11 años
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Resumen del Recurso
Immunoglobulins
5 classes
Ig A
Secretory- dimeric
has SC that protects in harsh enviroment of secretions
2 subclasses IgA1/A2
Serum-monomeric
Ig D
Very low serum concentrations
Found on lymphocyte surface
Function unclear
Ig G
Most abundant Ig in plasma
It has 4 subasses-IgG1/G2/G3/G4
Efficient at triggering complement and phagocytosis via Fc receptors
Only antibody to cross placenta to foetus
Predominant antibody in 2nd response
Ig M
Only in plasma and secretion too large to enter tissue
Pentamer, joined by J chains and disulphide bridges
Heavy chains has 5 domains
good at agglutinating particles e.g viruses, efficient at activating complement
Predominant antibody in 1st response
Ig E
Extra C domain
Associated with allergic response
Protects against parasites
Structure of antibody
Light chains have 2 types- Lambda and kappa
Fold up into 2 domaians-VL and CL, each domain made of 2 Beta sheets linksed b y a disulphide bridge
Heavy chain determines the class of the antibody
Fold into 4(5) domains-VH, CH1,CH2,CH3 (CH4)
Fab- responsible for binding the antigen
Fc-reponsible for effector function (clearance mechanisms)
How are antigens recognised?
3 hypervariable loobs (CDR) in each variable domain (VH & VL) form the antigen binding site
Antibody recognises structural epitopes on the antigen
Binds antigen with non- covalent interactions
Effect of Antibodies
Blocking of entry to pathogens
Antibody binds to virus preventing it binding with receptors so preventing fusion event
Antibodies against adhesion bind to bacterial and prevent colonization and therefore uptake
Neutralisation of toxins
IgG and IgA bind to solube toxin preventing them from binding to cellular receptors and poisoning the cell
Activation of classical complement pathway (IgM or Ig G) which leads to bacterial cell lysis
IgM binds to antigens on bacterial surface, adopt staple form. C1q complex binds to IgM and activates C1r which cleaves and activates serine protease
IgG bind to antigens on bacterial surface. C1q cmplx binds to at least 2 IgG molecules. This activates C1r which cleaves and activates serine protease
Bacterial opsonisation
1) Bacterial is coated in complement and antibody
2) When complement bind to receptor and the antibody binds to the Fc receptor on macrophage membrane the bacteria is phagocytosed
3) Macrophage membrane fuse forming a phagosome
4) Lysosomes fuse with hagosome and release enzymes that degrade the bacteria
Fc mediated clearance through cross-links
Aggregation of antibody on bacterial surface allows cross-llinking of Fc receptor and activation of macrohage, leading to phagocytosis and destruction
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