Paper No.

: 10 Immunology

Module : 2 Antigen recognition by immune cells – Adaptive immunity,

Antibody

Development Team
Principal Investigator: Prof. Neeta Sehgal
Head, Department of Zoology, University of Delhi

Paper Coordinator: Prof. Anju Srivastava

Department of Zoology, University of Delhi

Content Writer: Dr. Rajni Arora

Swami Shraddhanand College, University of Delhi

Content Reviewer: Prof. Sukhmahendra Singh

Banaras Hindu University

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 Description of Module

Subject Name ZOOLOGY

Paper Name Immunology; Zool 010

Module Name/Title Antigen recognition by immune cells – Adaptive immunity, Antibody

Module Id 2; Antigen recognition by immune cells

Keywords Immunity, adaptive, antibody, antigen, epitope, light chain, heavy

chain, B lymphocyte, T lymphocyte, humoral immunity, isotypes,
effector function

Contents
1. Learning Outcomes
2. Introduction
3. Adaptive Immunity
4. Antibody
4.1. Unique features of tool of humoral immunity: antibody
4.2. Important discoveries /research work in the field of antibody
4.3. Structure of antibody: light chain, heavy chain, J chain, Hinge region, disulphide bond,
carbohydrate group
4.3.1 Experiment of Tiselius and Kabat
4.3.2 Experiment of Rodney Porter and G. M. Edelmann
4.4 Structure of antibody (Light chains, heavy chains, J chain, hinge region, carbohyrate group,
disulphide bond)
5. Types of antibody
5.1. IgG
5.2. IgM
5.3. IgA
5.4. IgE
5.5. IgD
6. Functions of Antibody
6.1. Opsonisation
6.2. Complement activation
6.3. Antibody mediated cell cytotoxicity ADCC
6.4. Transcytosis
6.5. Passive immunity
7. Summary

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 1. Learning Outcomes

The study of the chapter will help in understanding the following:

 What is adaptive immunity?

 How is the structure of antibody deduced?
 Why is it an important component of adaptive immunity?
 How it is a component of antigen recognition unit?
 What are the various isotypes of antibody?
 How do the antibodies function to combat the pathogen?

2. Introduction

The chapter focuses on the biology of antibody which is an important effector molecule of the
humoral adaptive immunity. Antibodies or immunoglobulins which were earlier called magic bullets
are released in millions on activation of B lymphocytes. The study of structural detail of the molecule
is important to understand its function which is of great help to customize and manipulate it
commercially for various diagnostic and therapeutic uses. The important attributes of specificity and
diversity gives it the convenience to act at the strategic locations targeting variety of antigens entering
through different routes. The antibody is not only released in the body fluids but is also located on the
B cells as membrane receptors where it is a part of antigen recognition unit of B cell. The magic of the
antibody is clarified once we analyse its role as a static molecule on the B cells (mIg) and a mobile
effector molecule in blood and other secretions.

3. Adaptive Immunity

The adaptive immunity is given by the activation of two types of cells in the blood that is B and T
lymphocytes. These specialized cells are named on the basis of their immunological training in the Bone
marrow or Thymus respectively. Adaptive immunity is also called acquired immunity as it starts after
the exogenous or endogenous antigen enters and infects the body. B cell attacks the exogenous (outside)
antigen and T cell is deputed for endogenous (inside) antigen (Figure 1). It starts a few days after
infection as it gives the first chance to the innate mechanisms to provide the first line of defense.
Adaptive immunity has three important roles of recognizing, eliminating and remembering the pathogen
by producing few memory cells (Figure 2). It also has the power of giving immunity specific to the
antigen due to presence of different receptors that is BCR and TCR located on B and T cells. It is called
acquired immunity as it is a specialized defense mechanism which adapts on acquiring infection. The
existence of two different types of lymphocytes that is B and T lymphocytes was first reported by J. A.
Pierre Miller and G. F. Mitchell in 1966. Both the lymphocytes work efficiently in a co-operative
manner to give humoral and cell mediated immunity. The response given by B cells is called humoral
and the response given by T lymphocytes is called cell mediated. There are two subpopulations of T
cells called T helper or Th and T cytotoxic cells or Tc where Th cells decides what is to be activated that
is cell mediated immunity or humoral immunity. There is another subpopulation of T cells called T-
suppressor cells (Ts). They are the negative regulators of immunity and suppress the immune response if
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Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 there is over reaction in the body or reaction for self proteins. They are thus called immunoregulator
cells. The mature B or T cell which waits for encounter with the antigen for the first time is called Naïve
lymphocyte. Adaptive immunity differs from innate immunity in its antigenic specificity and presence
of memory cells. The memory cell membrane has the same receptors as the activated lymphocyte but
recognizes the antigen faster, if, it dares to enter the body again.

Figure 1: B and T cells

Figure 2: Showing Naive B cell and memory B cell

Source: www. en.wikipedia.org

4. Antibody

All the vertebrates are gifted with the ability to form large sized multifunctional glycoprotein called
antibody for giving the protection against the invading antigens. It is released in the blood and other
body fluids like milk, saliva, tears etc. because of which this type of immune response is called humoral
immunity (in Latin humor means fluid). The term antibody has originated from the German word
Antikorper. It was first coined by Von Behring and Kitasato in 1890 to describe an agent in blood that
was capable of passively transferring the immunity. They suggested that there exist an entity which
could act against the (anti) offending toxin. The antibodies may be located on the membranes of the B
cells or they may be secreted. The membrane bound antibody (mIg) acts as a receptor on the B cells
(BCR) for Ag recognition and the secreted form is for neutralization, clumping, precipitation and
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 agglutination etc. of Ag. The antibody present on the B cell makes it antigen specific (Figure 3) by
recognizing epitopes present on the antigen and activating the same cell after the signal is transduced.
The B cell is also an antigen presenting cell where it first endocytose the antigen and display it with the
membrane molecule MHCII. It is then activated by cytokines of Th cells. The B cell once activated
proliferates and produces clones of antigen specific B cells which finally changes into the antibody
secreting plasma cells (Figure 4). The antibodies try to inactivate, neutralize, agglutinate, precipitate and
clump the microbes so that they may not multiply and colonise in the organs they invade.

Figure 3: Antibody showing antigen specificity

Source: Wikimedia.Org

.
Figure 4: Activated B cell
Source: www Wikipedia.org
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 4.1. Unique features of tool of humoral immunity: antibody

 Antibody is an immunoglobulin.
 Antibody is an adaptor molecule as it is a bridge between antigen and effector molecule.
 Antibody is a glycoprotein.
 Antibody is a heterodimer.
 Antibody is an effector molecule.
 Antibody is specific to a single epitope
 Antibody in the serum is heterogenous.
 Antibody can act as antigen. Antibody raised against antibody is called anti-antibody.
 Antibody is of five types varying in the effector functions.
 Antibody can be monomeric or polymeric.
 Antibody is monoclonal and polyclonal.
 Antibody is a flexible molecule.
 Antibody is of two types: Membrane bound and Secretory.
 Membrane antibody is for antigen recognition as BCR.

4.2. Important discoveries/ research in the study of antibodies

 P. Ehrlich, 1900: Antibodies are magic bullets to target human disease and gave selection theory
of antigen and antibody.
 E. Von Behring: Serum antitoxins. Got Nobel Prize in 1901
 Arne Tiselius and Elvin Kabat: Antibodies are serum proteins/immunoglobulins. Discovered in
1939
 Karl Landsteiner 1940: Demonstrated that antibodies are specific in their recognition by using
hapten.
 Eisen and Karush in 1940 showed that antibody is divalent.
 L. Pauling and D. Pressman 1945 suggested that there are pockets in antibodies where antigen
binds and the interaction between the two is non covalent.
 Rodney Porter and G. Edelman gave chemical structure of antibody. Got Nobel Prize in1972.
 G. Edelman in 1970 showed that heavy chains are involved in effector function of antibody.
 Wu and Kabat in 1970 identified the hyper variable region on the antibody.
 Cesar Milstein, George Kohler, Neil Jerne: Monoclonal antibody. Got Nobel Prize in 1984
 Susuma Tonegawa: gene rearrangement in antibody production. Got Nobel Prize in 1987.
 Timosi T.B: Biological function of Ig A
 D. Rowe and J. Fahey: Biological function of Ig D
 O. Prausnitz and H. Kustner: PK reaction to study allergy (IgE).

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 4.3. Landmark experiments to study the anatomy of antibody

4.3.1. Experiment of Tiselius and Kabat

A. Tiselius and E.A. Kabat in 1939 worked on immunized rabbits by using the technique of
electrophoresis. By this technique the proteins on the gel when subjected to the electric current are
separated according to their size (Figure 5). They immunised the rabbit with the antigen ovalbumin.
Ovalbumin (OVA) a storage protein (45KDa) of Fowl egg is a good immunogen for the mammals due
to its large size and easy availability for immunization. They took the serum of the immunized rabbit
and divided it into two parts before electrophoresis. Out of the two parts which were electrophoresed,
one part was mixed with ovalbumin before electrophoresis. The second part of serum which was not
mixed with ovalbumin showed four peaks corresponding to albumin and α, β, γ globulin, but in the
serum mixed with ovalbumin the gamma peak in the graph was absent. They concluded that the
antibodies are in the gamma globulins fraction and hence named gamma globulin or immuno
globulins. With the advancement in electrophoretic technology, it is known that IgG the major
antibody exist in gamma fraction but alpha and beta globulins also contain other classes of antibody.

Figure 5: Electrophoretic separation of serum proteins to show the presence of immunoglobulins

4.3.2. Experiment of Rodney Porter and G. M. Edelmann

The insight into the structure of antibody was given by Rodney Porter and Gerald M Edelmann for
which they shared the Nobel Prize in Physiology in 1972, though they worked independently on the
molecular structure of the antibody (presentation speech). The large protein immunoglobulin was
broken using different enzymes like pepsin and papain (by R. Porter) and reducing agents like
Mercaptoethanol (2ME), (by G.M. Edelmann). The results were then compiled to deduce the Y
shaped structure of antibody. Pepsin cleaved the immunoglobulin at site of aromatic aminoacids like
tyrosine, tryptophan and phenyalanine resulting in two Fab and one Fc parts but the cleavage site of
papain (enzyme obtained from papaya latex) is at the cysteine residues. The cleavage product of
papain was a single piece with two Fab components. The Fc fragment was digested by the enzyme

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 completely. Mercaptoethanol broke the secondary and tertiary structure of the protein by reducing the
disulphide bonds thus releasing the polypeptide chains of two different sizes called as light and heavy
chains (Figure 6). The large heavy chain was of 55 KDa but the light chain was of 22KDa. A variety
of antibody types was listed by deciphering the amino acid sequences. The amino acid sequence of the
antibody was studied using cancerous plasma cell called myeloma cells. Variation in the amino acid
sequence of the light chains was later obtained using Bence jones (BJ) proteins. Bence Jones proteins
are immunoglobin light chains (22-24KDa) produced by the neoplastic plasma cells. They clumped
when heated at high temperature. Based on the studies of BJ proteins, there are two types of light
chains, called kappa and lambda differing in the constituition of constant regions. The heavy chains
and the light chains both have variable and constant regions. The constant regions of heavy chains are
of five types determining the five classes of antibodies as IgM, IgG, IgD, IgE and IgA.

Figure 6: Effect of proteolytic enzymes and mercaptoethanol on antibody

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 4.4. Structure of antibody (Light chains, heavy chains, J chain, hinge region, carbohydrate group,
disulphide bond)

Light chain and heavy chain

The antibodies are proteins made of four polypeptide chains, the two large sized of 55KDa each are
called heavy chains and the small sized polypeptide of 25KDa called light chains (Figure 7). The two
different light and heavy chains organize to form a Y shaped three dimensional structure of the antibody
due to intra and inter disulphide bonds and other noncovalent interactions. The protein nature of Ab also
contributes to the two functionally different N and C-terminals with specific roles. N-terminal shows
variability in amino acid sequence compared to C-terminal of polypeptide. The region of the heavy and
light chain showing amino acid variation in each molecule is denoted as VL and VH and constant region
as CH and CL

Figure 7: Antibody structure

Source: Commons.wikimedia.org

The intrachain disulphide bonds at a regular interval of 110 aminoacids result in converting the
peptide chain in to a compact globular domain. Each light chain consists of a single constant domain
called as CL, whereas, the heavy chain has two or three constant domains called as CH1, CH1 and CH3.
(Figure 8 and 9)

Figure 8: Antibody domain structure

Source: Commons.wikipedia.org

Immunology
ZOOLOGY Antigen recognition by immune cells – Adaptive immunity,
Antibody
 Figure 9: Domains making heavy and light chain. Yellow and green are the light chains and blue and red
are the heavy chains
Source: www.wikipedia.org

The study of secondary and tertiary structure of Ab shows all the immunoglobulin domains have β
pleated sheets, each consisting of three or four strands of anti-parallel polypeptides connected by
loops of variable length. The two β pleated sheets are connected by the conserved disulphide bonds.
The characteristic protein motif found in immunoglobulins is called immunoglobulin fold. N –
terminal variation in composition of heavy and light chain facilitates the execution of humoral
response to a variety of antigens. Within the variable domains of light and heavy chains there are
short amino acid sequences with exceptional variability at three locations called hypervariable
regions. They are also called complementarity determining region or CDR as they are the regions
which protrude out to form the peptide loops giving a shape complementary to the shape of the
antigenic determinant/epitope. There are three CDRs named CDR1, CDR2 and CDR3 which cluster
to give the shape to the antigen binding site of antibody also termed as paratope. Ag-ab interaction
occurs at epitope of the antigen and paratope site of antibody. The rest of the variable region is called
the framework region as it provides a scaffold to hold the hypervariable regions in place.

There are two types of the light chains in the monomer of antibody called lambda (λ) and kappa (κ).
The names lambda and kappa represent the first letter in Greek of the two scientists Korngold and
Lipari who first discovered them. Combination of both types of light chains is present in each
individual but the percentage composition may vary in different species. There are five different types
of heavy chains named as α, µ, γ, δ, ε based on the difference in the constant region of the heavy
chain. The antibody with five different types of the heavy chains exist in an individual and are further
called classes/isotypes. Each isotype has not only a distinct physical and biological property but
differs in its effector functions. The antibody with α chain is called antibody A, with μ chain is called
antibody M and accordingly antibody G, D and E. The subisotypes of the heavy chains also exist due
to the small amino acid variation in the isotypes. α1, α2 are the subisotypes of antibody A and γ1, γ2,
γ3 and γ4 are the subisotypes of antibody G. The different isotypes and its subtypes vary in
performing effector functions like opsonisation, complement activation, neonatal immunity etc. Most
of the effector functions are mediated by the C- terminal of the heavy chain of the antibody as it binds
with the receptors (FcR) on the cells like NK, mast cells, phagocytes etc.

The antibody is also classified as monomeric and polymeric. Monomeric antibody has two binding
sites for an antigen but the multimeric antibody has more than two binding sites. This interaction of

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Antibody
 antibody with the antigen is possible because of flexibility in the two arms of the antibody by the
presence of the hinge region specially in the IgG, IgD and IgE. The antibody which is specific for a
single epitope is called monoclonal antibody. The human serum contains a cocktail of antibodies
specific for various antigens and is called polyclonal serum. The monoclonal antibodies are prepared
in vitro by hybridoma technology. They are used as therapeutic and diagnostic agents.

Source www.wikipedia.org
Value addition: Antibodies are used in therapeutics to treat various diseases

Hinge region: The hinge region is located between CH1 and CH2 domains of the antibody (Fig 10). It
is mainly made of two types of amino acids that is proline and cystine which are vulnerable to the
attack by the proteolytic enzyme like papain. The proline amino acids provides the flexibility to the
arms of Ab but the cystine amino acid helps in forming the interchain disulphide bonds. The hinge
allows the two antigen binding Fab region of each antibody molecule to operate independently so that
it can bind antigen epitopes which are distantly separated. Though the arms are flexible but this
flexibility also hinders in saturating all the binding sites of the multimeric antibody. IgG3 has the
longest hinge region amongst the subtypes of IgG. The hinge region varies in length from 10 to 60
amino acids approximately.

J Chain: These are small proteins coded by different genes which connect the units of the polymeric
immunoglobulin. It is a joining chain with a molecular weight of approximately 15KDa and is linked
by the disulphide bond to the C- terminal of the heavy chains.

Disulphide bond: Heterodimeric antibody has intra and interchain disulphide bonds between the
peptide chains which give stability to its three dimensional Y shaped molecular structure.

Carbohydrate group: The immunoglobulins are glycosylated which means the carbohydrate moiety
is attached to it which is important for the passage of the antibody through the biological membranes
and placental barriers. All the isotypes have a different half life. The shortest half life is of IgE that is
of two days, IGA of three days, IgM of four days and IgG has longest half life of 21-28 days. The
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 long life of IgG is attributed to the FcRn (neonatal Fc receptor) which protects it from lysosomal
degradation for a long time.

Figure 10: Structure of Antibody (modified)

5. Types of Antibody

The five different types of antibodies (IgG, IgM, IgA, IgE, IgD) perform different biological functions
and each type is important so as to kill or inactivate the pathogen entering through various routes in
the body (Figure 12 and Table 1).

5.1. IgG

The IgG is monomeric antibody having the highest concentration in the serum. It constitutes about
80% of the total serum concentration.It is a good complement activator, can cross placenta and gives
the passive immunity to the foetus. It also mediates the opsonization process by the macrophages and
the neutrophils. Based on the minor aminoacid differences in the heavy chain, it has been divided in
four subclasses namely IgG1, IgG2, IgG3, and IgG4. There is difference in the number of disulphide
bonds and the size of the hinge region in the subclasses of the isotype IgG. Out of the four subtypes,
IgG1 is best in giving passive immunity to the foetus and in mediating the process of opsonization.
IgG3 is the best activator of complement. Its concentration is less in the primary immune response but
increases in the secondary immune response.

5.2. IgM

It is the antibody present on both the cell membrane and in secretions. The membrane bound antibody
is monomeric but the secretory form is pentameric. Though it can bind with ten epitopes but there is
steric hindrance as a result it can interact with the maximum of six or seven epitopes. It is existing in the
serum with only 5-10% of the total concentration and a very less amount exist in the mucosal secretions.
It is the antibody for the primary response as it appears first in response to the infection. The pentameric

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 secretory form of IgM helps to attack the pathogen quickly. It can not cross the placental barrier due to
its polymeric nature. It is the first antibody to be produced by the neonate. The five monomers of the
antibody are linked to each other by the joining chain or J chain. The J chain is synthesized in the
plasma cell. The J chain also helps in transport of the antibody across the epithelial layers as mucosal
secretion. It is the best complement activator and forms big aggregates of agglutination. It is also
important to know that the IgM also include Isohaemagglutinins which are the naturally occurring
antibodies against the red blood cell antigens and thus determine the ABO blood group system (Figure
11). These antibodies might have originated as a result of some bacteria entering through the various
routes as discussed earlier. These bacteria had antigenic determinants similar to the oligosaccharide
antigen of the ABO Blood group. Thus without the immunization of individuals, anti-A or anti-B or
both may be present in the blood as given in the Fig11. The pentameric nature of IgM does not allow it
to cross the placenta so incompatibility of ABO is not dangerous to mother and foetus.

Figure 11: ABO Blood group

Source: www. commons wikimedia.org

5.3. IgA

It is the type of antibody which exist in the serum and in the mucosal secretions of the respiratory,
gastrointestinal and urinogenital tract. It is dimeric, trimeric or tetrameric in its secretory form. It is
mostly transported as dimeric form. It is also assisted by the J chain for the polymerization and for the
transport to the mucosal surface. It is important as it coats the antigen and prevents its attachment to
the mucosal layers. Thus for protection against local infections, routes of immunizations causing local
production of IgA is better than those producing antibody in serum. As the complement receptors are
absent on IgA molecule so it is not a complement activator.

5.4. IgE

It is present in very less concentration in the serum but, is biologically very potent to induce
hypersenstive reaction against an allergen. It is named antibody E because of the antigen E present on
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 the ragweed pollen. The presence of this antibody was first detected by Prausnitz and Kusner in 1921
and the reaction is also called PK reaction. It binds to the Fc receptors present on the membranes of
basophils and mast cells .The cross linking of the allergen with the antibody bound to Fc receptors on
the same cell results in giving the signal for the degranulation of the pharmacologically active
reagents which cause a reaction like wheal and flare or hives etc.

5.5. IgD

It is present as membrane bound antibody on the mature B cells. It acts as a receptor on B cells so
called BCR. Its biological function is not very clear. It is less than 5% of total serum immunoglobins.

Table 1: Types of antibody and their properties

Source: www.wikimedia.org

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 IgM , IgD

Figure 12: Types of antibody showing secretory and membrane bound

Source: Spot Pcc.Edu modified diag

6. Functions of Antibody

The two different components of Ab that is the Fab and Fc are for epitope –paratope interaction and
effector function respectively. The various functions of antibody are:

6.1. Opsonization

It is the coating of the antibody on the surface of the antigen due to the epitope - paratope interaction which
makes the antigen more vulnerable to attack by both the phagocytic and nonphagocytic cells (Figure 13 and
14). The phagocytic cells like macrophages and neutrophils and some non-phagocytic cells have the receptors
(FcR) for binding with the FC of antibody. This interaction results in initiating the signal transduction pathway
for the different mechanisms of the phagocytic activity for the secured killing of the pathogen.

Figure 13: Opsonisation Figure 14: Opsonisation (animated form)

Source: www.en.wikipedia.org

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 6.2. Complement activation

Complements are the set of serum proteins which when activated make perforations in membrane of
pathogen and finally kill it (Figure 15).

Figure 15: Complement activation

Source: commons Wikimedia.org

6.3. Antibody mediated cell cytotoxicity ADCC

The natural killer cells (NK) are activated for its cytotoxic function by the antigen- antibody
interactions as these cells have the Fc receptors on their membranes. (Figure 16)

Figure 16: ADCC

Source: www.en.wikipedia.org

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 6.4. Transcytosis

The Fc component of Ab assists in transfer of the antibody from the epithelial layer to the mucosal
surface of the gastrointestinal, respiratory and the urogenital tracts. It binds with the polyIg receptor
on the basolateral side of the epithelial cell which is endocytosed and then excreted in the mucosal
surface.

6.5. Passive immunity

The growing embryo in the mother’s body that is fetus is protected by passive immunity as IgG is
selectively transported across the placenta mediated by neonatal Fc receptors (FcRn). Maternal
immunogen is also transferred to the offspring through the transport of IgG across the gastrointestinal
tract.

Ag and Ab interactions involve four types of non- covalent interactions making it a reversible reaction
(Figure 17). Antibodies can also become potent immunogen and can induce immune response. Based
on the difference in light and heavy chains they are classified as isotypes, allotypes and idiotypes.
Isotypes are due to difference in the constant regions of heavy chains and are species specific. The
allotypes are due to the allelic difference in the genes resulting in variation in the amino acids in the
constant domains of the heavy and light chains. The idiotypes may arise due to the difference in the
aminoacids in the variable portions of the heavy and light chains

Figure 17: Showing Ag-Ab forces (modified)

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 Figure 18: Affinity and Avidity: Pentameric antibody showing avidity

The binding strength of a single epitope and paratope is called affinity but the total strength of
interaction of multiple epitopes and multivalent antibody is called avidity. Since the antibody can
bind 2-10 epitopes of an antigen the total strength is more than affinity of single antigen and antibody
(Figure 18).

Some hot spots in the antibody research are designer Ab, chimaeric Ab, Antibody as
immunosensor etc

Source: www.genscript.com

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 7. Summary

 Antibody is the important effector molecule of the adaptive immune system.

 It is a Y shaped glycoprotein with Fab and Fc components.
 It has diversity as it is specific to variety of antigens which are encountered in the blood and other
body fluids.
 It is both membrane bound and secretory.
 Membrane bound antibody is for recognition of antigen and is part of recognition unit called
BCR.
 Each component of Ab that is, light and heavy chain, hinge region, disulphide bonds, J chain and
carbohydrate group gives it special properties and makes it a versatile molecule.
 It has five isotypes as IgA, IgM, IgG, IgD and IgE.
 Each type functions at strategic locations of the body.
 The various effector functions like ADCC, complement activation, opsonisation etc aim to target
the antigen and differ in isotype and sub isotype.
 The Ag- Ab interactions are noncovalent and occur at the epitope of antigen and paratope of
antibody.

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