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TABLE OF CONTENT
OBJECTIVE
 TYPES OF ANTIBODIES
INTRODUCTION:
Antibodies are proteins produced and secreted by B cells. They bind to foreign substances that
invade the body, such as pathogens.

The term “antibody” refers to its function, which is to bind to an antigen. Another name for this
protein molecule is immunoglobulin (abbreviated Ig).
Antibodies are Y-shaped molecules, consisting of two heavy chains (H chains) and two light
chains (L chains) arranged as shown in the diagram on the right.
FUNCTIONS OF ANTIBODIES:
Antibodies have three main functions, which are as under:
 Neutralization
 Punching Holes in the cell wall
 Oponization

NEUTRALIZATION:
Antibodies are secreted into the blood and mucosa, where they bind to and inactivate
foreign substances such as pathogens and toxins

PUNCHING HOLES IN CELL WALL:

Antibodies activate the complement system to destroy bacterial cells by lysis (punching holes in
the cell wall).

OPSONIZATION:
Antibodies facilitate phagocytosis of foreign substances by phagocytic cells
ANTIBODIES AND FOUR KEY FEATURES OF THE IMMUNE SYSTEM:
1-SPECIFICITY OF ANTIBODIES:
Antibodies exactly recognize toxins and pathogens.

2- DIVERSITY OF ANTIBODIES:
Antibodies against a variety of antigens preexist in the body.
3- IMMUNOLOGICAL MEMORY:
We don’t don’t develop symptoms of measles

4. Immune tolerance: Self cells and tissues are not normally

attacked.
The specificity of antibodies
Each antibody recognizes
one specific antigen.
For example, an antibody
that recognizes the
mumps virus cannot
recognize the measles
virus. Conversely, an
antibody that recognizes
the measles virus cannot
recognize the mumps
virus. This feature is
called “antibody
specificity.”

Each B cell (antibody-

producing cell) produces one kind of antibody. However,
pathogens produce millions of harmful factors.
Then, how does the body defend itself against countless
harmful factors?

The diversity of antibodies and immunological memory

Tens to hundreds of millions of different B cells are circulating in the body so that every antigen is recognized.
In other words, the body is prepared for the invasion of pathogens by possessing B cells that produce unique
antibody molecules. This feature is called “antibody diversity.”

After an infection, the cells producing pathogen-specific antibodies multiply and increase proportionally. As a
result, the body is protected from repeated infection. This feature is called “immunological memory.”

Structure and characteristics of antibody isotypes

Human antibodies are classified into five isotypes (IgM, IgD, IgG, IgA, and IgE) according to their H chains,
which provide each isotype with distinct characteristics and roles.
IgG
IgG is the most abundant antibody isotype in the blood (plasma),
accounting for 70-75% of human immunoglobulins (antibodies). IgG
detoxifies harmful substances and is important in the recognition of
antigen-antibody complexes by leukocytes and macrophages. IgG is
transferred to the fetus through the placenta and protects the infant
until its own immune system is functional.
IgM
IgM usually circulates in the blood, accounting for about 10% of
human immunoglobulins. IgM has a pentameric structure in which
five basic Y-shaped molecules are linked together. B cells produce IgM
first in response to microbial infection/antigen invasion.
Although IgM has a lower affinity for antigens than IgG, it has higher
avidity for antigens because of its pentameric/hexameric structure.
IgM, by binding to the cell surface receptor, also activates cell
signaling pathways.
IgA
IgA is abundant in serum, nasal mucus, saliva, breast milk, and
intestinal fluid, accounting for 10-15% of human immunoglobulins.
IgA forms dimers (i.e., two IgA monomers joined together). IgA in
breast milk protects the gastrointestinal tract of neonates from
pathogens.
IgE
IgE is present in minute amounts, accounting for no more than
0.001% of human immunoglobulins. Its original role is to protect
against parasites. In regions where parasitic infection is rare, IgE is
primarily involved in allergy.
IgD
IgD accounts for less than 1% of human immunoglobulins. IgD may be
involved in the induction of antibody production in B cells, but its
exact function remains unknown.

Immunoglobulin class switching

B cells expressing plasma membrane-bound IgM and IgD (mature B
cells) are activated upon encounter with a specific antigen, and begin
to proliferate and produce secretory IgM and IgD. With further
activation by the antigen or other stimuli, these mature B cells
differentiate into cells that produce increasing amounts of secreted
immunoglobulins, and start to produce immunoglobulin isotypes
other than IgM and IgD. This process is called “immunoglobulin class
switching”.
Factors in the B cell environment (including hormones secreted by T
cells [cytokines]) direct the isotype switching.
Examples
Interleukin 4 (IL4) stimulates class switching from IgM/IgD to IgG1
and IgE
Interleukin 5 (IL5) stimulates class switching from IgM/IgD to IgA
*Interleukins are a type of cytokine that is produced by leukocytes and
lymphocytes during the immune response.

antibody structure
The four-chain structure of an antibody, or immunoglobulin, molecule. The basic unit is composed of
two identical light (L) chains and two identical heavy (H) chains, which are held together by disulfide
bonds to form a flexible Y shape. Each chain is composed of a variable (V) region and a constant (C)
region.

DEFINITION:
Antibody, also called immunoglobulin, a protective protein produced by the immune system in
response to the presence of a foreign substance, called an antigen.
FUNCTION:
Antibodies recognize and grip onto antigens in order to remove them from the body. A wide
range of substances are regarded by the body as antigens, including disease-causing organisms
and toxic materials such as insect venom.

What Are Antibodies?

Antibodies, also known as immunoglobulins, are Y-shaped proteins that are produced by the
immune system to help stop intruders from harming the body. When an intruder enters the body, the
immune system springs into action. These invaders, which are called antigens, can be viruses,
bacteria, or other chemicals. When an antigen is found in the body, the immune system will create
antibodies to mark the antigen for the body to destroy.

Function
The antibodies act sort of like the immune system's scouts. They find antigens, stick to them, and
identify for the immune system the exact type of antigen so that it can be destroyed. Each antibody
is made for one and only one antigen, and it's fitted with special receptors that will only bind to that
antigen. For instance, a specific antibody is created to help destroy the chickenpox virus. Only that
particular antibody will attack a chickenpox virus.

How Antibodies Fight Antigens

So what happens when an antigen tries to enter the body? When it does, the immune system is
triggered. Chemical signals are sent to alert all the different parts of the immune system into action.
First, the virus is met by a type of cell called B cells. The B cells are responsible for creating
antibodies to match the antigen. Remember, each type of antibody matches to only one antigen.
After the B cells have created their antibodies, the antibodies stick to the virus, marking it for the next
round of attack. T cells are then ordered to attack the antigen that the antibodies have marked for it.
After the antigen has been destroyed, the cleanup crew comes along. A wave of phagocytes, large
cells that can consume foreign matter, eats the remains of the infection.

Immunizations
After an infection is defeated, the antibodies still remain in the body. They are left there to wait in
case that particular antigen returns. For example, after a person gets chickenpox, the antibody that
was created by the immune system to get rid of the chickenpox will remain in the body. The next
time the chickenpox virus tries to invade the patient, the antibody will be ready. It will instantly attach
to the virus, calling the T cells and phagocytes much quicker, and stopping the infection much
earlier.
Immunizations take advantage of the fact that antibodies remain in the body after an infection is
eradicated. Most immunizations consist of a weak or diluted form of an antigen - not enough of the
antigen to make the patient sick, but just enough to trigger the creation of antibodies. This way, the
body can instantly attack any form of the infection it encounters, stopping the infections before they
begin.
Types Of Antibodies
In total, there are five types of antibodies. Each type is found in a different part of the body and has a
different set of duties. Each one of them is referred to by a letter following the abbreviation Ig for
immunoglobulin.
The most common antibody we have is the IgG antibody. IgG is found in all of the body's fluids. It
makes up about 75-80% of all of our antibodies. These antibodies help to fight off bacteria and
viruses. To go with the flow of the fluids, IgG antibodies are the smallest antibodies in size.
The biggest in size are the IgM group, found in the lymphatic and circulatory systems. The IgMs are
the first responders, the first type of antibodies to confront invaders to these two systems.
• An antigen can be defined as a
substance that, when introduced into
the circulation of an individual lacking
that antigen, can stimulate the
production of a specific antibody.

antibody can be defined as a protein (i.e. an immunoglobulin with specific antigen binding sites)
produced as a result of the introduction of a foreign antigen, that has the ability to combine with (and,
in many cases, destroy) the cells carrying the antigen that stimulated its production.

When an unfamiliar substance enters the body, the immune system is

able to recognize it as foreign because molecules on the surface of the
antigen differ from those found in the body. To eliminate the invader,
the immune system calls on a number of mechanisms, including one
of the most important—antibody production. Antibodies are produced
by specialized white blood cells called B lymphocytes (or B cells).
When an antigen binds to the B-cell surface, it stimulates the B cell to
divide and mature into a group of identical cells called a clone. The
mature B cells, called plasma cells, secrete millions of antibodies into
the bloodstream and lymphatic system.

As antibodies circulate, they attack and neutralize antigens that are

identical to the one that triggered the immune response. Antibodies
attack antigens by binding to them. The binding of an antibody to
a toxin, for example, can neutralize the poison simply by changing its
chemical composition; such antibodies are called antitoxins. By
attaching themselves to some invading microbes, other antibodies can
render such microorganisms immobile or prevent them from
penetrating body cells. In other cases the antibody-coated antigen is
subject to a chemical chain reaction with complement, which is a
series of proteins found in the blood. The complement reaction either
can trigger the lysis (bursting) of the invading microbe or can attract
microbe-killing scavenger cells that ingest, or phagocytose, the
invader. Once begun, antibody production continues for several days
until all antigen molecules are removed. Antibodies remain in
circulation for several months, providing extended immunity against
that particular antigen.

antigen; antibody; lymphocyte

Phagocytic cells destroy viral and bacterial antigens by eating them, while B cells produce antibodies
that bind to and inactivate antigens

B cells and antibodies together provide one of the most important

functions of immunity, which is to recognize an invading antigen and
to produce a tremendous number of protective proteins that scour the
body to remove all traces of that antigen. Collectively B cells recognize
an almost limitless number of antigens; however, individually each B
cell can bind to only one type of antigen. B cells distinguish antigens
through proteins, called antigen receptors, found on their surfaces. An
antigen receptor is basically an antibody protein that is not secreted
but is anchored to the B-cell membrane. All antigen receptors found
on a particular B cell are identical, but receptors located on other B
cells differ. Although their general structure is similar, the variation
lies in the area that interacts with the antigen—the antigen-binding, or
antibody-combining, site. This structural variation among antigen-
binding sites allows different B cells to recognize different antigens.
The antigen receptor does not actually recognize the entire antigen;
instead it binds to only a portion of the antigen’s surface, an area
called the antigenic determinant or epitope. Binding between the
receptor and epitope occurs only if their structures are
complementary. If they are, epitope and receptor fit together like two
pieces of a puzzle, an event that is necessary to activate B-cell
production of antibodies.
Each antibody molecule is essentially identical to the antigen receptor
of the B cell that produced it. The basic structure of these proteins
consists of two pairs of polypeptide chains (lengths of amino acids
linked by peptide bonds) that form a flexible Y shape. The stem of the
Y consists of one end of each of two identical heavy chains, while each
arm is composed of the remaining portion of a heavy chain plus a
smaller protein called the light chain. The two light chains also are
identical. Within particular classes of antibodies the stem and the
bottom of the arms are fairly similar and thus are called the constant
region. The tips of the arms, however, are highly variable in sequence.
It is these tips that bind antigen. Thus each antibody has two identical
antigen-binding sites, one at the end of each arm, and the antigen-
binding sites vary greatly among antibodies.
variable and constant domains of an antibody
Variable (V) and constant (C) domains within the light (L) and heavy (H) chains of an antibody, or
immunoglobulin, molecule. The folded shapes of the domains are maintained by disulfide bonds
(―S―S―).