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IMMUNOGLOBULIN 
S 
Dr. Humera Kausar 
2014 
Immunology lecture # 5
Antibodies 
 Proteins that recognize and bind to a particular antigen 
with very high specificity. 
 Made in response to exposure to the antigen. 
 Each antibody has at least two identical sites that bind 
antigen: Antigen binding sites.
Antibody Structure 
An antibody molecule is composed of two identical heavy 
chains (H) and two identical light chains (L), each with a 
variable region (V)  constant region (C).
45 kDa 
50 kDa
100kDa
Antibody Structure 
Immunoglobulins are glycoproteins made up of: 
- Four polypeptide chains (IgG): 
a- Two light (L) polypeptide chains 
b- Two heavy (H) polypeptide chains 
- The four chains are linked by disulfide bonds 
- Terminal portion of L-chain contains part of antigen binding site 
- Terminal portion of H-chain participate in antigen binding site 
- H-chains are distinct for each of the five Immunoglobulins 
- The other (Carboxyl) terminal portion forms Fc fragment
Antibody Structure
Fine Structure of Antibody
Five classes of Antibodies: 
* IgG 
 IgM 
 IgA 
 IgD 
 IgE
Immunoglobulin Classes 
I. IgG 
Structure: Monomer 
Percentage serum antibodies: 80% 
Location: Blood, lymph, intestine 
Half-life in serum: 23 days 
Complement Fixation: Yes 
Placental Transfer: Yes 
Known Functions: Enhances phagocytosis, 
neutralizes toxins and viruses, protects fetus 
and newborn.
IgG ---- BIOLOGICAL ACTIVITY 
 IgG1, IgG3  IgG4 readily cross the placenta and 
play an important role in protecting the developing 
fetus. 
 IgG3 is the most effective complement activator, 
followed by IgG1, IgG2 is less efficient and IgG4 is not 
able to activate complement at all.
IgG ---- BIOLOGICAL ACTIVITY 
IgG1 and IgG3 bind with high affinity to Fc receptor 
on phagocytic cells and mediate opsonization. 
IgG4 has an intermediate affinity for Fc receptors, 
and IgG2 has an extremely low affinity.
Immunoglobulin Classes 
II. IgM 
Structure: Pentamer 
Percentage serum antibodies: 5-10% 
Location: Blood, lymph, B cell surface 
(monomer) 
Half-life in serum: 5 days 
Complement Fixation: Yes 
Placental Transfer: No 
Known Functions: First antibodies produced 
during an infection. Effective against microbes 
and agglutinating antigens.
1st Ig class produced in primary response to an antigen 
and also 1st Ig to be synthesized by the neonate. 
 More efficient than IgG at activating complement. 
 Secreted by plasma cells as a pentamer. plays an 
important accessory role as a secretory immunoglobulin. 
 Five monomer units are held together by disulfide 
bonds that link their carboxyl-terminal heavy chain 
domains.
IgM --------- BIOLOGICAL ACTIVITY 
Each IgM pentamer contains additional Fc linked 
polypeptide called J-Chain, which is –S-S- bonded to 
the carboxyl-terminal cystein residue of two of the ten 
μ chains. 
 J-Chain required for polymerization of monomers 
to form pentameric IgM. 
 J-Chain is added just before secretion of the 
pentamer. 
 Presence of J-Chain allows IgM to bind to receptors 
on secretory cells, which transport it across epithelial 
lining to enter the external secretions that bathe 
mucosal surface.
Immunoglobulin Classes 
III. IgA 
 Structure: Dimer 
 Percentage serum antibodies: 10-15% 
 Location: Secretions (tears, saliva, intestine, 
milk), blood and lymph. 
 Half-life in serum: 6 days 
 Complement Fixation: No 
 Placental Transfer: No 
 Known Functions: Localized protection of 
mucosal surfaces. Provides immunity to infant 
digestive tract.
Major Secretory Ig, present in saliva, tears, 
milk, and mucus of bronchial, genitourinary  
digestive tracts. 
 Secretory IgA consists of a dimer or tetramer, 
a j-chain polypeptide and a polypeptide chain 
called secretory component.
IgA ---- BIOLOGICAL ACTIVITY 
J-Chain polypeptide in IgA is identical to that 
found in pentameric IgM  serves similar 
function in facilitating the polymerization of 
both serum IgA and secretory IgA. 
 Secretory component (70 kDa) consists of 5 
Ig like domains.
IgA --- BIOLOGICAL ACTIVITY 
Domains of secretory polypeptide binds to the 
domains of IgA dimer and stabilized by a disulfide 
bond. 
 Every day , a human secretes 5 to 15 g of 
secretory IgA in to mucous secretions.
Immunoglobulin Classes 
IV. IgD 
 Structure: Monomer 
 Percentage serum antibodies: 0.2% 
 Location: B-cell surface, blood, and lymph 
 Half-life in serum: 3 days 
 Complement Fixation: No 
 Placental Transfer: No 
 Known Functions: In serum function is unknown. 
On B cell surface, initiate immune response.
 Major membrane bond immunoglobulin expressed 
by mature B cells. 
 Its role in the physiology of B cells is under 
investigation. 
 No biological effector function has been identified 
for IgD.
Immunoglobulin Classes 
V. IgE 
 Structure: Monomer 
 Percentage serum antibodies: 0.002% 
 Location: Bound to mast cells and basophils 
throughout body. Blood. 
 Half-life in serum: 2 days 
 Complement Fixation: No 
 Placental Transfer: No 
 Known Functions: Allergic reactions. Possibly 
lysis of worms.
 IgE mediate the immediate hypersensitivity 
reaction / allergic reaction. 
 Ragweed pollen is a potent inducers of this class 
of Ab. 
 IgE binds to Fc receptors on the membranes of 
Basophils and tissue mast cells.
Cross linkage of receptor bound IgE 
molecules by Ag (allergens) induces Basophils 
 mast cells to translocate their granules to 
the plasma membranes  release contants to 
the extracellular enviornment 
(degranulation).
Antibodies 
Function 
Protective outcomes of 
antibody-antigen binding 
› Neutralization 
 Prevents toxin from interacting with 
cell 
› Immobilization and prevention 
of adherence 
 Antibody bonding to cellular 
structures to interfere with function 
› Agglutination and precipitation 
 Clumping of bacterial cells by 
specific antibody 
 Bacteria more easily phagocytized
Antibodies 
Function 
 Protective outcomes of 
antibody-antigen binding 
› Opsinization 
 Coating of bacteria with antibody to 
enhance phagocytosis 
› Complement activation 
 Antibody bonding triggers classical 
pathway 
› Antibody-dependent cellular 
cytotoxicity 
 Multiple antibodies bind a cell which 
becomes target for certain cells
ا وہی ہے جس نے تمہیں مٹی سے پیدا 
کیا پھر ایک وقت مقرر کر دیا اور اس 
کےہاں ایک مدت مقرر ہے تم پھر بھی 
( شک کرتے ہو ( 2 
سُورَۡةُ اٴلنعَام

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5th immunoglobulins 2 oct 2014

  • 1. IMMUNOGLOBULIN S Dr. Humera Kausar 2014 Immunology lecture # 5
  • 2. Antibodies Proteins that recognize and bind to a particular antigen with very high specificity. Made in response to exposure to the antigen. Each antibody has at least two identical sites that bind antigen: Antigen binding sites.
  • 3. Antibody Structure An antibody molecule is composed of two identical heavy chains (H) and two identical light chains (L), each with a variable region (V) constant region (C).
  • 4. 45 kDa 50 kDa
  • 6. Antibody Structure Immunoglobulins are glycoproteins made up of: - Four polypeptide chains (IgG): a- Two light (L) polypeptide chains b- Two heavy (H) polypeptide chains - The four chains are linked by disulfide bonds - Terminal portion of L-chain contains part of antigen binding site - Terminal portion of H-chain participate in antigen binding site - H-chains are distinct for each of the five Immunoglobulins - The other (Carboxyl) terminal portion forms Fc fragment
  • 8. Fine Structure of Antibody
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  • 10. Five classes of Antibodies: * IgG  IgM  IgA  IgD  IgE
  • 11. Immunoglobulin Classes I. IgG Structure: Monomer Percentage serum antibodies: 80% Location: Blood, lymph, intestine Half-life in serum: 23 days Complement Fixation: Yes Placental Transfer: Yes Known Functions: Enhances phagocytosis, neutralizes toxins and viruses, protects fetus and newborn.
  • 12. IgG ---- BIOLOGICAL ACTIVITY  IgG1, IgG3 IgG4 readily cross the placenta and play an important role in protecting the developing fetus.  IgG3 is the most effective complement activator, followed by IgG1, IgG2 is less efficient and IgG4 is not able to activate complement at all.
  • 13. IgG ---- BIOLOGICAL ACTIVITY IgG1 and IgG3 bind with high affinity to Fc receptor on phagocytic cells and mediate opsonization. IgG4 has an intermediate affinity for Fc receptors, and IgG2 has an extremely low affinity.
  • 14. Immunoglobulin Classes II. IgM Structure: Pentamer Percentage serum antibodies: 5-10% Location: Blood, lymph, B cell surface (monomer) Half-life in serum: 5 days Complement Fixation: Yes Placental Transfer: No Known Functions: First antibodies produced during an infection. Effective against microbes and agglutinating antigens.
  • 15.
  • 16. 1st Ig class produced in primary response to an antigen and also 1st Ig to be synthesized by the neonate.  More efficient than IgG at activating complement.  Secreted by plasma cells as a pentamer. plays an important accessory role as a secretory immunoglobulin.  Five monomer units are held together by disulfide bonds that link their carboxyl-terminal heavy chain domains.
  • 17. IgM --------- BIOLOGICAL ACTIVITY Each IgM pentamer contains additional Fc linked polypeptide called J-Chain, which is –S-S- bonded to the carboxyl-terminal cystein residue of two of the ten μ chains.  J-Chain required for polymerization of monomers to form pentameric IgM.  J-Chain is added just before secretion of the pentamer.  Presence of J-Chain allows IgM to bind to receptors on secretory cells, which transport it across epithelial lining to enter the external secretions that bathe mucosal surface.
  • 18. Immunoglobulin Classes III. IgA Structure: Dimer Percentage serum antibodies: 10-15% Location: Secretions (tears, saliva, intestine, milk), blood and lymph. Half-life in serum: 6 days Complement Fixation: No Placental Transfer: No Known Functions: Localized protection of mucosal surfaces. Provides immunity to infant digestive tract.
  • 19. Major Secretory Ig, present in saliva, tears, milk, and mucus of bronchial, genitourinary digestive tracts.  Secretory IgA consists of a dimer or tetramer, a j-chain polypeptide and a polypeptide chain called secretory component.
  • 20.
  • 21.
  • 22. IgA ---- BIOLOGICAL ACTIVITY J-Chain polypeptide in IgA is identical to that found in pentameric IgM serves similar function in facilitating the polymerization of both serum IgA and secretory IgA.  Secretory component (70 kDa) consists of 5 Ig like domains.
  • 23. IgA --- BIOLOGICAL ACTIVITY Domains of secretory polypeptide binds to the domains of IgA dimer and stabilized by a disulfide bond.  Every day , a human secretes 5 to 15 g of secretory IgA in to mucous secretions.
  • 24. Immunoglobulin Classes IV. IgD Structure: Monomer Percentage serum antibodies: 0.2% Location: B-cell surface, blood, and lymph Half-life in serum: 3 days Complement Fixation: No Placental Transfer: No Known Functions: In serum function is unknown. On B cell surface, initiate immune response.
  • 25.  Major membrane bond immunoglobulin expressed by mature B cells.  Its role in the physiology of B cells is under investigation.  No biological effector function has been identified for IgD.
  • 26. Immunoglobulin Classes V. IgE Structure: Monomer Percentage serum antibodies: 0.002% Location: Bound to mast cells and basophils throughout body. Blood. Half-life in serum: 2 days Complement Fixation: No Placental Transfer: No Known Functions: Allergic reactions. Possibly lysis of worms.
  • 27.  IgE mediate the immediate hypersensitivity reaction / allergic reaction.  Ragweed pollen is a potent inducers of this class of Ab.  IgE binds to Fc receptors on the membranes of Basophils and tissue mast cells.
  • 28. Cross linkage of receptor bound IgE molecules by Ag (allergens) induces Basophils mast cells to translocate their granules to the plasma membranes release contants to the extracellular enviornment (degranulation).
  • 29. Antibodies Function Protective outcomes of antibody-antigen binding › Neutralization  Prevents toxin from interacting with cell › Immobilization and prevention of adherence  Antibody bonding to cellular structures to interfere with function › Agglutination and precipitation  Clumping of bacterial cells by specific antibody  Bacteria more easily phagocytized
  • 30. Antibodies Function  Protective outcomes of antibody-antigen binding › Opsinization  Coating of bacteria with antibody to enhance phagocytosis › Complement activation  Antibody bonding triggers classical pathway › Antibody-dependent cellular cytotoxicity  Multiple antibodies bind a cell which becomes target for certain cells
  • 31. ا وہی ہے جس نے تمہیں مٹی سے پیدا کیا پھر ایک وقت مقرر کر دیا اور اس کےہاں ایک مدت مقرر ہے تم پھر بھی ( شک کرتے ہو ( 2 سُورَۡةُ اٴلنعَام