Immunoglobulin

Immunoglobulins

Igs are glycoproteins, produced in response to an immunogen by plasma

cells and function as antibodies

+ -
Amount of protein

albumin

globulins
Immune
α1 α2 β γ serum

Ag-adsorbed
serum
Mobility
 Antibodies
Similar in overall structure;
• 2 identical H & 2 L-chains
• H – chains roughly twice
larger than L–chains Disulfide bond

• Disulfide bonds
• L- and H - chains in any Carbohydrate
single Ig - protein are identical
• Constant and Variable regions
• Ag binding site: VH and VL CL
collectively make Fab
(antigen binding fragment) VL

CH2 CH3
CH1
Hinge Region
VH
 Ig Structure

• L & H chains contain a series of repeating,

homologous units which fold independently: Disulfide
common globular motif – Ig domain bond

• L-chains always contain 2-domains,

Carbohydrate
while H–chains may contain 4-5

  and  chains contain 4 domains

C
  and  chain are made up of 5-globular V L

domains L

CH CH
• Hinge Region CH
2 3
1 Hinge Region
V
H
 Immunoglobulin Fragments:
Structure/Function Relationships

Ag Binding

Complement Binding Site

Binding to Fc
Receptors
Placental Transfer
 Human Immunoglobulin Classes

Despite similarities, Abs are divided (size, charge, solubility)

into distinct classes and subclasses
- On the basis of heavy chain:
• IgG - Gamma (γ)
• IgM - Mu (µ)
• IgA - Alpha (α)
• IgD - Delta (δ)
• IgE - Epsilon (ε)
 Human Immunoglobulin Subclasses

• IgG Subclass
– IgG1 - Gamma 1 (γ1)
– IgG2 - Gamma 2 (γ2)
– IgG3 - Gamma 3 (γ3)
– IgG4 - Gamma 4 (γ4)

• IgA subtype
– IgA1 - Alpha 1 (α1)
– IgA2 - Alpha 2 (α2)
 Light chain

• Kappa () and Lambda ()

• There is no known functional difference
• One Ig molecule always contain  or  chains, never a mixture
• In humans (:) ratio is 2:1
 Abs: Molecules for immune effector system

a. Activate C’ – lysis & phagocytosis of microbes

b. Binds to Ag – enhance phagocytosis
c. Recognition of target
d. Stimulates degranulation of mast cells & release mediators
e. Cross placental barrier
 Immunoglobulin Fragments:
Structure/Function Relationships

Papain

Fab

Fc

Fab
 Immunoglobulin Fragments:
Structure/Function Relationships

Pepsin

F(ab’)2 Fc Peptides
 IgG
• Structure
– Monomer (7S)

IgG1, IgG2 and IgG4 IgG3

 IgG

• Structure
• Properties
– Major serum Ig (systemic immunity)
– Placental transfer
– Fixes complement
– Binds to receptors
• Phagocytes - opsonization
 IgM
J Chain
• Structure
– Pentamer (19S)
– Extra domain
(CH4)
Cµ4
– J chain
 IgM
• Structure
• Properties
– 3rd highest serum Ig
– First Ig made by fetus and B cells
– Fixes complement
 IgM
• Structure
• Properties
– 3rd highest serum Ig
– First Ig made by
fetus and B cells
– Fixes complement

–Binds to Fc receptors
–B cell surface Ig
Tail
Piece
 IgA
• Structure
– Secretions (sIgA)
• Dimer (11S)
• J chain
• Secretory
component

Secretory Piece J Chain

Origin of Secretory Component of
sIgA
 IgA
• Structure
• Properties
– 2nd highest serum Ig
– Major secretory Ig (Mucosal or Local Immunity)
• Tears, saliva, gastric and pulmonary secretions
– Does not fix complement
– Binds to Fc receptors on some cells
 IgD

• Structure
– Monomer
– Tail piece

Tail Piece
 IgD
• Structure
• Properties
– 4th highest serum Ig
– B cell surface Ig
– Does not bind complement
 IgE

• Structure
– Monomer
– Extra domain
(CH4)

Cε4
 IgE
• Structure
• Properties
– Least common serum Ig
• Binds to basophils and mast cells
– Allergic reactions
– Parasitic infections
– Does not fix complement
Thank you