IgG & IgA

IgG & IgA (Immunoglobulin G and
Immunoglobulin A for biochemistry)
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HUSSAIN ALI ADAWAILAH
ID|101-1-22
Immunoglobulin G (IgG)
 This is responsible for the major part of the immunity against blood borne
infectious agents.
 It has the highest concentration of 8-16 mg/mL in normal adult serum as
compared to all other classes of the immunoglobulins. It has four different
sub classes:
 IgG1, IgG2, IgG3, IgG4
 These different classes differ slightly in the amino acid sequences in a
particular region called constant region in the H-chain (We will look at the
different polypeptide chains of immunoglobulins shortly).
 These differences are reflected in their functional activities. Ig is the only
immunoglobulin which can cross the placental barrier and thus provides
passive humoral immunity to the developing foetus.
IgG Structure:
 All IgG immunoglobulins have a four chain structure
 This 4 chain structure of IgG is in fact the basic structural unit present in all classes of
the immunoglobulins
Antibodies have 5 different kinds of heavy chains called µ, δ, γ, ε and α chains. These
Hchains are present in IgM, IgD, IgG, IgE and IgA respectively and distinguish these different
classes of antibodies/immunoglobulins.
 In the subclases of IgG the heavy chains are different and are called γ1, γ2,
γ3, γ4 and belong to the respective sub classes.
 The molecular weights of the H-chain in IgG is in the range of 50-55 kDa. In
any given immunoglobulin molecule, the two heavy chains and the two light
chains are identical, giving an antibody molecule two identical antigen-
binding sites, and thus the ability to bind simultaneously to two identical
structures.
 Immunoglobulins have two different kinds of light chains. These two L-chains
are called κ (kappa) and λ (lambda). Each has a molecular weight of 23 kDa. A
given immunoglobulin either has κ chains or λ chains, never one of each. No
functional difference has been found between antibodies having λ or κ light
chains, and either type of light chain may be found in antibodies of any of the
five major classes.
 The two heavy chains are linked to each other by disulfide bonds and each
heavy chain is linked to a light chain by a disulfide bond.
 These intramolecular disulphide bridges create compact structural units
called domains.
 These domains are shown in the Figure below as VH, VL, CH1 , CH2 , CH3 .
The domains are also sometimes called as regions.
 The IgG molecule consists of two symmetrical units joined by one interchain
disulphide
Fab and Fc fragments

 The N-terminal half of the H-chain and all of the L-chain are also connected with an
interchain disulphide bridge.
 This part of the molecule is called Fab fragment.
 The subscript ab refers to the fact that this portion has the binding site for the
antigen.
 Thus „ab‟ subscript refers to antigen binding property of the fragment F. As the
immunoglobulin molecule is symmetrical, each IgG has 2 Fab fragments.
The Fc Fragment
 The three quarter of the H-chains from the C-terminal side and the C-
terminal half of the Lchains are constant. All antibodies of the same class and
sub class have the same amino acid sequence. Hence these regions have
been denoted as CH with C referring to constant. The C-terminal half of each
H-chain constitutes Fc fragments. The subscript „c‟ refers to the fact that it
was found to be easily crystallizable for X-ray diffraction studies. Thus Fc
stands for fragment crystallized.
 Fc fragment is not involved in the antigen binding but binds to complement and
some other cells of the immune system
 There is a hinge region around the place where Fab fragments join the Fc fragment.
This is more flexible region and provides the required flexibility to the two Fab
fragments to move with respect to each other
Further work by Michael Green and Robert Valentine showed that another protease pepsin
cleaved Ig differently.
Hypervariable regions
 The following Kabat and Wu plot shows the variability of the amino acid
sequences in both H-chains and L-chains among different antibodies.
 The different antibodies are against different antigens/antigenic
determinants. Hence the variability is the origin of the antibody specificity.
 Hypervariable regions constitute the antigen binding sites. Affinity labeling
confirmed the existence of hypervariable regions. Reactive haptens were
found to react to the antigen binding sites (the hypervariable regions).
 Hypervariable regions are called complementarity determining regions
(CDRs).
IgA
 It also has two subclasses IgA1 and IgA2 with identical molecular weight of
160 kDa.
 The subclasses have α1 and α2 as H-chains.
 The concentration of IgA1 in human serum is much higher than IgA2.
 IgA protects the mucous membranes and is present in all secretions as the
most abundant Ig.
 In those specie in which IgG is not transferred across the placenta, It is IgA
which protects neonates.
 It is present in colostrums. IgA can form dimmers and polymers.
 It is present in humans as monomers only and mostly as dimmers in other
animals.
 It contains a secretory component SC and a joining chain (J-chain). SC
stabilizes IgA and is involved in its transport of exocrine IgA. J-chain helps in
the dimerization of secretory IgA (dimeric).

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IgG & IgA (Immunoglobulin G and

Immunoglobulin A for biochemistry)

Fab and Fc fragments

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