 An antibody (Ab), also known as an

immunoglobulin (Ig), is a large Y-shaped protein

produced by B-cells that is used by the immune system
to identify and neutralize foreign objects such as
bacteria and viruses.
 The antibody recognizes a unique part of the foreign
target, called an antigen. Each tip of the "Y" of an
antibody contains a paratope (a structure analogous
to a lock) that is specific for one
particular epitope(similarly analogous to a key) on an
antigen, allowing these two structures to bind together
with precision.
 The paratope is the part of an antibody which
recognizes an antigen, the antigen-binding site of an
antibody.
 An epitope, also known as antigenic determinant, is
the part of an antigen that is recognized by
the immune system, specifically by antibodies, B cells,
or T cells.
 Antibodies are heavy (~150 kDa) globular plasma
proteins. They have sugar chains added to some of
their amino acid residues. In other words, antibodies
are glycoproteins.
 Antibodies are secreted by a type of white blood cell
called a plasma cell
 The production of antibodies is the main function of
the humoral immune system
STRUCTURE OF ANTIBODY:
Disulfide bond

Carbohydrate

CL

VL

CH2 CH3
CH1

Hinge Region
VH
STRUCTURE OF ANTIBODY
 1. Fab region
2. Fc region
3. Heavy chain (blue)
with one variable (VH)
domain followed by a
constant domain (CH1),
a hinge region, and two
more constant (CH2
and CH3) domains.
4. Light chain (green)
with one variable (VL)
and one constant (CL)
domain
5. Antigen binding site
(paratope)
6. Hinge regions.
 1. HEAVY AND LIGHT CHAINS :
 All immunoglobulins have a four chain structure as their
basic unit.
 They are composed of two identical small light chains
(23kD) and two identical large heavy chains (50-70kD)
 Heavy Chain:
 There are five types of mammalian Ig heavy chain denoted by
the Greek letters: α, δ, ε, γ, and μ.
 The type of heavy chain present defines the class of antibody;
these chains are found in IgA, IgD, IgE, IgG, and IgM
antibodies, respectively
 Light Chain:
 In mammals there are two types of immunoglobulin light
chain, which are called lambda (λ) and kappa (κ).
 2.DISULFIDE BONDS
 The heavy and light chains and the two heavy chains are
held together by inter-chain disulfide bonds
 3.VARIABLE (V) AND CONSTANT (C) REGIONS
 The heavy and light chain could be divided into two
regions based on variability in the amino acid sequences.
 These are the:
 1. Light Chain - VL (110 amino acids) and CL (110 amino
acids)
 2. Heavy Chain - VH (110 amino acids) and CH (330-440
amino acids)
 Most H chains consist of one variable (VH) and three
constant(CH) domains.(IgG and IgA have three CH
domains,whereas IgM and IgE have four.)
 The variable regions are responsible for
antigenbinding ,whereas the constant regions are
responsible for various biologic functions
eg, complement activation and binding to
cell surface receptors.
 4.Fab Region:
 The arms of the Y contain the sites that can bind two
antigens (in general, identical) and, therefore,
recognize specific foreign objects. This region of the
antibody is called the Fab (fragment, antigen
binding) region. It is composed of one constant and
one variable domain from each heavy and light chain
of the antibody
 5.Fv Region:
 The paratope is shaped at the amino terminal end of
the antibody monomer by the variable domains from
the heavy and light chains. The variable domain is also
referred to as the FV region and is the most important
region for binding to antigens.
 6. Fc Region:
 The base of the Y plays a role in modulating immune
cell activity. This region is called the Fc (Fragment,
crystallizable) region.
 the Fc region ensures that each antibody generates an
appropriate immune response for a given antigen, by
binding to a specific class of Fc receptors.
CLASSES OF IMMUNOGLOBINS:
 The immunoglobulins can be divided into five
different classes, based on differences in the amino
acid sequences in the constant region of the heavy
chains.
 1. IgG – Gamma(γ) heavy chains
 2. IgM – Mu(μ) heavy chains
 3. IgA – Alpha(α) heavy chains
 4. IgD – Delta(δ) heavy chains
 5. IgE – Epsilon(ε) heavy chains
IgG
 Structure: Monomer (7s)

IgG1, IgG2 and IgG4 IgG3

Properties:
 IgG Is the Major Antibody in the Blood, but It Is Able
to Enter Tissue Spaces and Coat Antigens, Speeding
Antigen Uptake
 Molecular weight: 150,000
 H-chain type (MW): gamma (53,000)
 In its four forms, provides the majority of antibody-based
immunity against invading pathogens. The only antibody
capable of crossing the placenta to give passive immunity
to the fetus
 Fixes complement - Not all subclasses fix equally well; IgG4
does not fix complement
 Representing approximately 75%
of serum immunoglobulins in humans, IgG is the
most abundant antibody isotype found in the
circulation.
IgG consists of four subclasses (isotypes),
which are
numbered in order of their serum concentrations
(IgG1, IgG2, IgG3, and IgG4)
 IgG molecules are synthesized and secreted
by plasma B cells.
 Binds to Fc receptors on phagocytic cells.
 IgG is the predominant immunoglobulin in blood,
lymph, peritoneal fluid, and cerebrospinal fluid.
IgM:
 Structure
 Pentamer (19S)
composed of 5 H2L2
units plus one molecule
of J chain
Extra domain (CH4)
 J chain-This chain
functions in
polymerization of the
molecule into a
pentamer.
Properties of IgM:
 3rd highest serum Ig
 IgM is the first antibody to appear during an immune
response and the first formed by a developing fetus.
 IgM acts as one of the main receptors on the surface of
mature B cells, along with IgD. When IgM is a surface
receptor, it is in its monomeric form.
 First Ig made by fetus and B cells
 IgM is the most versatile antibody and almost certainly
the first type of immunoglobulin to have developed
evolutionarily.
 As a consequence of its pentameric structure, IgM is a
good complement fixing Ig. Thus, IgM antibodies are
very efficient in leading to the lysis of microorganisms.
 Produced early in the primary response
 The most efficient Ig.
 because of the J chain, it is also important as a
secretory immunoglobulin
 Since secretory immunoglobulins are present in breast
milk as well, IgM also participates significantly in
protecting the newborn from intestinal pathogens
IgA:
 Serum - monomer
 Secretions (sIgA)
 Dimer (11S), sIgA molecule consists of two H2L2
units plus one molecule each of J chain and
secretory component(SC or SP)

Secretory Piece J Chain

Properties of IgA
 2nd highest serum Ig
 the IgA which is made in the plasma cell, the
secretory piece is made in epithelial cells and is
added to the IgA as it passes into the secretions .
The secretory piece helps IgA to be transported
across mucosa and also protects it from
degradation in the secretions.
 Major secretory Ig ( saliva, tears, respiratory,
intestinal, and genital tract secretions.)
 Does not fix complement unless aggregated
 Binds to Fc receptors on some cells
IgD:
 Structure
 Monomer
 Tail piece

Tail Piece

 Properties
 4th highest serum Ig
 B cell surface Ig
 Does not bind complement
IgE:
 Structure
 Monomer
 Extra domain (CH4)

 Properties CH4
 Least common serum Ig
 Allergic reactions
 Parasitic infections
 Does not fix complement
Summary of functions:
 IgG: In its four forms, provides the majority of antibody-based
immunity against invading pathogens. The only antibody capable of
crossing the placenta to give passive immunity to fetus.
 IgM: Expressed on the surface of B cells (monomer) and in a secreted
form (pentamer) with very high avidity. Eliminates pathogens in the
early stages of B cell mediated (humoral) immunity before there is
sufficient IgG
 IgA: Found in mucosal areas, such as the gut, respiratory tract and
urogenital tract, and prevents colonization by pathogens.Also found in
saliva, tears, and breast milk.
 IgD: Functions mainly as an antigen receptor on B cells that have not
been exposed to antigens.It has been shown to activate basophils and
mast cells to produce antimicrobial factors.
 IgE: Binds to allergens and triggers histamine release from mast cells
and basophils, and is involved in allergy. Also protects against parasitic
worms.