Course: Clinical Immunology

Course Instructor : Qurrat Ul Ain Malik

Semester: 4th (Medical Laboratory Technology)
Topic: Immunoglobulins
 IMMUNOGLOBULINS

• Antibodies (Ab)/Immunoglobulins (Ig) are gamma-globulin

proteins that react specifically with the antigen that stimulated
their production.

• Make up about 20% of the protein in blood plasma.

• There are five classes of antibodies: IgG, IgM, IgA, IgD, and
IgE based on differences in their heavy chains.
 FUNCTIONS OF IMMUNOGLOBULINS

a. Neutralization of toxins and viruses

b. Opsonization of microbes

c. Activation of complement system

d. Prevention of the microbial attachment to mucosal surfaces.

e. Catalytic (enzymatic) capability

IMMUNOGLOBULINS
 IMMUNOGLOBULIN STRUCTURE

• Y shape protein structure made up of four polypeptide chains:

1. Two L chains :light (L)(MW 25,000)

2. Two H chains :heavy (H)(MW 50,000 to 70,000)

• 4 chains are linked by disulfide bonds.

• Ab molecule consists of identical H chains and identical L chains

by the result of two phenomena:
a. Allelic exclusion

b. Regulation within the B cell

 IMMUNOGLOBULIN STRUCTURE

• L chain consists of a variable region and a constant region.

• H chain consists of a variable region and a constant region (CH1,

CH2, and CH3).

– CH2 domain contains the complement-binding site

– CH3 domain is the site of attachment of IgG to receptors on

neutrophils and macrophages.
 IMMUNOGLOBULIN STRUCTURE

• The antigen binding site is formed by the variable regions of both

the light and heavy chains.

• The specificity of the antigen-binding site is a function of the

amino acid sequence of the hypervariable regions.
IMMUNOGLOBULIN STRUCTURE
IMMUNOGLOBULINS
IMMUNOGLOBULINS
 IMMUNOGLOBULINS

IgG: (2H2L)
• 2 identical antigen-binding sites-divalent

• 4 subclasses, IgG1–IgG4, based H chains and disulfide bonds.

IgG1(65%) of the total IgG.

• Predominant antibody in the secondary response

• Can cross the placenta; most abundant immunoglobulin in

newborns.

• Can activate complement & opsonizes.

 IMMUNOGLOBULINS

IgM: (2H2L) a μ heavy chain

• Main Ig primary response. Present as a monomer on the surface

of virtually all B cells and in serum, present as pentamer
composed of five H2L2 units plus one molecule of J (joining)
chain. IgM has.

• Most efficient immunoglobulin in agglutination,

• Highest avidity of the immunoglobulins

IMMUNOGLOBULINS
 IMMUNOGLOBULINS

IgA:

• Found in secretions (colostrum, saliva, tears, and respiratory,

intestinal, and genital tract secretions).

• Prevents attachment of microbes to mucous membranes.

• Consists of 2 H2L2 units + 1J (joining) chain3 and secretory

component. 2α H chains.
 IMMUNOGLOBULINS

IgE: (0.002%)

• Mediates immediate (anaphylactic) hypersensitivity by basophils

and mast cells.

• Participates in host defenses against certain parasites (e.g.,

helminthes/worms (Strongyloides, Trichinella, Ascaris, and the
hookworms Necator and Ancylostoma) by eosinophils.

• Bound IgE serves as a receptor for antigen (allergen).

• IgE doesn’t fix complement and doesn’t cross the placenta.

 IMMUNOGLOBULINS

Polyclonal Antibodies:

• Antibodies that arise in response to typical antigens are

heterogeneous, because they are formed by several different
clones of plasma cells. They will have the affinity for the same antigen
but different epitopes.

Monoclonal Antibodies:

• Antibodies that arise from a single clone of cells (e.g., in a plasma

cell tumor (myeloma)) are homogeneous.
IMMUNOGLOBULINS
 TYPES OF ANTIBODIES

1. Precipitin: An Ab that produces a visible precipitate when it

reacts with its Ag.

2. Lysin: An Ab able to cause lysis of cells (especially bacteria).

3. Agglutinoid: An agglutinin that has lost or never had the power

to agglutinate but can still unite with its agglutinogen.
 COMPLEMENT PROTEINS

Reference Book
Chap 59-Microbiology and Immunology by Levinson.
THANK YOU