Antibody Structure and Funcion

Antibody Structure and Function.
 Antibodies are immunoglobulins (Ig) which are produced by mature B-cells

(plasma cells) where they can be secreted or membrane bound
 They are soluble and circulate freely.
 They are used for immunity and protection against foreign materials
 Igα and Igβ associated with B-cell receptors.
 Structure
 An antibody molecule is composed of two identical Ig heavy chains (H) and
two identical light chains (L), each with a variable region (V) & constant region
(C).
 The papain cleavage splits the antibody into three equal fragments.
 The two fragments can bind antigens but cannot precipitate it.
 Fab region ( Fragment antigen binding region)
 3rd fragment ( Fc- fragment crystallization) cannot bind to antigen.
K or λ
 Anatomy of light (L) and heavy (H) chain:
 L- chain:
 L- chain of antibody is composed of about 220 aminoacids.

 Around 100-110 aminoacids are located at N-terminal (amino-terminal) and the
aminoacids sequences varies among antibodies. This region of L-chain is
known as variable (V) region.
 Remaining 110 aminoacids located at C-terminal (carboxyl-terminal) of L-chain
are almost constant among antibodies. This region of L-chain is known as
constant (C) region. Two types of constant region sequences are found ie.
Lambda (λ) and Kappa (κ). In a particular antibody either 2 lambda or 2 kappa
chains are present but not 1 lambda and kappa
 H-chain:
 In H-chain about 110 aminoacids are located at N-terminal which shows great
variation among antibody. This region is known as Variable (V) region.
 Remaining aminoacid sequences of H-chain is somewhat constant but reveals
five different types of constant (C) heavy chain region ie.(GAMED) Gamma γ,
Alpha α, Mu μ, Epsilon ε and Delta δ
 Antibodies molecules are classified into five classes on the basis of constant
region of H-chain.
IgM Mu
IgG Gamma
IgA Alpha
IgD Delta
IgE Epsilon
 Domain structure of antibody:
 Two domains are found in L-chain ie one in variable region (VL) and other in
constant region (CL).
 In H-chain, one domain is found in Variable region (VH). In IgA, IgG and IgD
three domains are found in constant region (CH1, CH2 and CH3) whereas in
IgE and IgM fou domains are found in constant region of H-chain (CH1, CH2,
CH3 and CH4.
Fab, Fc and Hinge region of antibody:
 Fab region
 In an antibody molecule two Fab regions are found and they binds antigens.
 The aminoacid seq varies amoung different antibodies. This determines the
specificity of the antibody
 Hypervariable region on L-chain (VL domain) and H-chain (VH domain) form
antigen binding site.
 VH region has high ratio of different amino acids in any given positon.
 VH region (paratop) directly contact the position of the antigen surface
( epitope)
 Antigen binding site is complementary to epitope of antigen, so it is also known
as complementary determining regions (CDRs).
 Fc region:
 Fc region of immunoglobulin allows for interaction of immune complex with

other phagocytic cells and complement.
 Take parts in various biological functions that are determined by aminoacid
sequences of each domains of constant region.
 Hinge region:
 Hinge region is rich in proline residue and is flexible. Therefore IgG, IgD and
IgA are flexible.
 The flexibility given by hinge region enable Fab region to assume various angle
to bind antigen.
Just for extra info: Characteristics of antibodies;

1. Antibodies are immunoglobulin (Ig) molecules
2. Antibodies are antigen specific and binds to foreign molecules to host.
3. They are produced by activated B-cells
4. Antibodies are first molecules participating in specific immune response
5. They mediate effector function to neutralize or eliminate foreign invaders.
 Immunoglobulin classes or Isotypes
Antibody belongs to class of protein called Immunoglobulin (Ig). And classified into 5
classes or isotypes
Ig chain type Abundance
IgG H chain= Gamma. Most abundant class in serum
Light chains = Kappa or (80%)
Lambda
IgM H chain = Mu 5-10% in serum
IgA H chain= alpha 10-15%
IgD H chain = delta Lowest conc. 0.2%
IgE H chain = Epsilon 0.3%
 IgG:
 It has longest half-life among other antibodies. Half-life is about 23 days.

 IgG is the only antibody that can cross placenta. It cross placenta and provide
immunity to fetus upto 6 month of age. The immunity is known as natural
passive immunity.
 It can also activate complement.
 Biological functions:
 Ig, IgG3 and IgG4 cross the placenta and play important role in protecting the
fetus.
 Make Antigen more attractive to phagocytes
 Causes agglutination of insoluble antigens and precipitation of soluble antigens
and helps in bacterial immobilization.
 neutralize toxin and viruses.
 Mediates opsonisation.
 Plays a role in antibody dependent cell mediated cytotoxicity (ADCC) ( refer to
innate immunity NK)
 Fab binds to the target cell
 Fc bind to NK cell
 Destroys target by releasing toxic substances containing cytoplasmic
granules.
 IgM:
 IgM is the first antibody produced in primary immune response and it is also
the first Ig produced by neonate
 IgM is secreted by plasma cell and it exists in pentameric form in which five
IgM mononers are linked together by disulphide bond (J-chain).
 Biological functions:
 IgM has higher valency (antigen binding ste) due to its pentameric form.
 Due to pentameric form, IgG is very effective in agglutination reaction.
 IgM is most efficient in complement activation.
 IgM plays important accessory role as secretory immunoglobulin due to J-
chain.
 Increases visibility of viruses/bacteria to phagocytes
 Rapidly reduces antigen concentration
 IgA:
 It is the predominant Immunoglobulin in external secretions such as breast

milk, saliva, tears and mucus of bronchial, genitourinary and digestive tracts.
 IgA primarily exists as monomeric in the serum (function unknown) but dimeric,
trimeric and some tetrameric form are also present.
 IgA in blood occurs in monomeric form whereas those in body secretion occurs
in dimeric or multimeric forms.
 Intestinal protection of neonate against pathogens during first week of life.
 Dimeric form of IgA contains J-chain and secretory chain. Secretory chains
helps in transcytosis.
 IgA can cross epithelial layer and enter into body secretion. The process of
crossing epithelial layer by IgA is known as transcytosis.
 Biological functions;
 IgA can cross the epithelial layer and enter into body secretion and provides
local immunity in GI tracts, respiratory tract, genital tract etc
 Bactericidal against Gram negative bacteria in the presence of lysozyme
 In body secretion IgA neutralize viruses and prevent attachment on host
surface.
 Efficient in agglutinating antibodies
 IgD:
 IgD together with IgM is the major membrane bound immunoglobulin
expressed on mature B-cell.
 Functions as antigen-specific receptor on B-cells
 Silences autoreactive B-cells
 IgE:
 IgE is also known as reagenic antibody due to its involvement in allergic

reaction. IgE mediate immediate hypersensitivity reaction and responsible for
symptoms like hay fever, asthma, anaphylactic shocks, etc.
 Fc region of IgE binds on blood basophils and tissue mast cells. The cross
reaction with antigen to Fc region bound IgE causes degranulation of mast cell
and basophils releasing histamine. Histamine is responsible for symptoms of
allergy.
 Biological functions;
 IgE provides immunity against parasite by Antibody dependent cell mediated
cytotoxicity (ADCC).
 Level of IgE antibody in blood of normal individual is very low and its level
increases during parasitic infection and in allergic reactions.
 Reaction may be mild ( mosquito bite) or severe (brinchial asthma)

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Antibody Structure and Function.

 Antibodies are immunoglobulins (Ig) which are produced by mature B-cells

 L- chain of antibody is composed of about 220 aminoacids.

 Domain structure of antibody:

 Fc region of immunoglobulin allows for interaction of immune complex with

Just for extra info: Characteristics of antibodies;

 Immunoglobulin classes or Isotypes

 It has longest half-life among other antibodies. Half-life is about 23 days.

 It is the predominant Immunoglobulin in external secretions such as breast

 IgE is also known as reagenic antibody due to its involvement in allergic

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