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Antibody and Antigen
Antibody and Antigen
By:
Thadly Chandra
Yestine Yuliantina
Overview of the Immune
Response
Antigen Definition
Is any substance that causes your
immune system to prompts the
generation of antibodies
Antigens can be proteins,
polysaccharides, conjugates of lipids
with : proteins (lipoproteins) and
polysaccharides (glycolipids)
An antigen may be a foreign substance
from the environment such as chemicals,
bacteria, viruses, or pollen.
An antigen may also be formed within
the body, as with bacterial toxins or
tissue cells.
Antigen
The body recognizes antigens by the three-
dimensional shapes or regions called antigenic
determinants or epitopes. Properties that make
molecules more effective antigens include:
Stable molecules, ie, molecules that assume and
maintain a definite shape
Larger molecules with molecular masses between
5000 and 100,000 daltons
Molecules that are structurally complex, with
distinctive shapes and novel subunit combiniations
Origin of Antigens
Antigens can be classified in order of their class
Exogenous antigens
Endogenous antigens
Autoantigens
Exogenous antigens
Exogenous antigens are antigens that have
entered the body from the outside, for example
by inhalation, ingestion, or injection.
Exogenous antigens (inhaled, ingested, or
injected) are taken up by antigen-presenting
cells (APCs)
The immune system's response to exogenous
antigens is often subclinical by endocytosis or
phagocytosis.
Endogenous antigens
Endogenous antigens are antigens that have
been generated within cells as a result of normal
cell metabolism, or because of viral or
intracellular bacterial infection.
Autoantigens
An autoantigen is usually a normal protein or
complex of proteins (and sometimes DNA or
RNA) that is recognized by the immune system
of patients suffering from a specific autoimmune
disease.
These antigens under normal conditions, not be
targeted of the immune system, but due to
mainly genetic and environmental factors, the
normal immunological tolerance for such an
antigen has been lost in these patients.
Antibody Structure
Antibodies are globular plasma proteins
They have sugar chains added to some
of their amino acid residues. In other
words, antibodies are glycoprotein
Produced by B-cell
Are antigen-specific
Bind and inactivate foreign particles
The basic functional unit of each
antibody is an immunoglobulin
Y-shaped molecule
Each antibody
consists of four
polypeptides - two
heavy chains and
two light chains
connected by
disulfide bonds,
joined to form a "Y"
shaped molecule.
Although the general structure of all
antibodies is very similar, a small region at
the tip of the Y varies greatly among
different antibodies
This variable region, composed of 110-130
amino acids, allowing millions of antibodies
with slightly different tip structures, or
antigen binding sites
The variable region includes the ends of
the light and heavy chains.
Each antibody binds to a specific antigen; an interaction similar
to a lock and key
Name Types Description
Antibody Isotypes IgA 2 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
Antibodies can come in IgD 1 Functions mainly as an antigen
different varieties known receptor on B cells that have not been
exposed to antigens. Its function is
as isotypes or classes. less defined than other isotopes.
The base of the Y plays a role in modulating immune cell activity. This region is
called the Fc (Fragment, crystallizable) region, and is composed of two
heavy chains that contribute two or three constant domains depending on the
class of the antibody.
By binding to specific proteins the Fc region ensures that each antibody
generates an appropriate immune response for a given antigen.
The Fc region also binds to various cell receptors, such as Fc receptors, and
other immune molecules, such as complement proteins.
1. Fab region
2. Fc region
3. Heavy chain 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 with one variable
(VL) and one constant (CL) domain
5. Antigen binding site (paratope)
6. Hinge regions.
Function
Antibodies contribute to immunity in three
ways:
they prevent pathogens from entering or
damaging cells by binding to them
they stimulate removal of pathogens by
macrophages and other cells by coating the
pathogen
they trigger destruction of pathogens by
stimulating other immune responses such as
the complement pathway
Antibody-Antigen Interaction
The interaction of the antibody with an antigen
causes a change in shape of the antibody
May cause the exposure of another site which
then is responsible for the various reactions
elicited by the antibody to destroy the foreign
substance.
The interaction of antibodies and antigens may
produce a network type complex.
The variable regions shown as black or gray in the
picture are the areas of the receptor site for the antigen.
NATURE OF ANTIGEN-ANTIBODY
REACTIONS
A. Lock and Key Concept
The combining site of an antibody is located in the Fab portion
of the molecule and is constructed from the hypervariable
regions of the heavy and light chains
B. Non-covalent Bonds
The bonds that hold the antigen to the antibody combining site
are all non-covalent in nature. These include hydrogen bonds,
electrostatic bonds, Van der Waals forces and hydrophobic
bonds.
C. Reversibility
Since antigen-antibody reactions occur via non-covalent bonds,
they are by their nature reversible.