Chapter 43

ANTIBODY
STRUCTURE & FUNCTIONS
5th Feb 2016
PowerPoint TextEdit Art Slides for
Biology, Seventh Edition

P.Buvanesh

Neil Campbell and Jane Reece

Levinson,
W.(2010) Review of Medical Microbiology & Immunology.(11th ed.).
The McGraw- Hill Companies.

Copyright 2005 Pearson Education, Inc. publishing as Benjamin Cummings

TOPIC LEARNING
OUTCOMEs

Able to define antibodies.

Able to list 5 classes of immunoglobulins and outline their characters.
Able to draw and label the basic molecular structure of Igs.
Able to describe the functions of various immunoglobulins.

B CELLS

1. B CELLS ARISE FROM BONE MARROW STEM CELLS.

2. MATURE B CELLS EXIT BONE MARROW AND ENTER THE CIRCULATORY SYSTEM.

3. B CELLS RECIRCULATE THROUGH LYMPHOID ORGANS IN SEARCH OF ANTIGEN.

B CELLS AND ANTIBODIES

Secreted
antibodies

BCR

Naive

Active

In the transition from nave to active B cells, the plasma cells secrete a
MODIFIED VERSION of the B CELL RECEPTOR.
This molecule is known as an antibody.
The BCR and corresponding antibody share IDENTICAL antigen
specificities.

What are Antibodies?

Antibodies (A.K.A. Immunoglobulin) are a type of
glycoprotein produced by B lymphocytes. Antibodies bind
antigen with a high degree of specificity and affinity.
Antibodies recognize a variety of three-dimensional shapes
(amino acids, lipids, carbohydrates, etc).

ANTIBODY STRUCTURE
An antibody consists of 4
polypeptides: 2 identical light chains
and 2 identical heavy chains form a
Y-shaped molecule.
Each light chain is connected to a
heavy chain by a disulfide bond and
the two heavy chains are connected
by two disulfide bonds.
Antigen binding and effector
domains are separated by a hinge
region. The hinge region allows the
two antigen binding domains to
move, enabling them to bind
antigens that are separated by
varying distances.

LIGHT CHAIN

HEAVY CHAIN

ANTIBODY STRUCTURE
ANTIGEN RECEPTORS HAVE
DISTINCT FUNCTIONAL DOMAINS
1. The variable (V) region varies
between clones and is involved in
antigen recognition.

2. The constant (C) region is

conserved among clones and is
required for structural integrity and
effectors functions.

ANTIBODY STRUCTURE
Each Light chain contains one V
domain and one C domain.
Each Heavy chain contains one V
domain and at least three C
domains.
Each domain folds into a
characteristic 3-D shape:
The Immunoglobulin (Ig)
domain.

VL

Antibodies bind antigens through the variable

regions of the light and heavy chains.
VH

ANTIBODY STRUCTURE
The unique structural architecture of antibodies allows multiple, highly
diverse antigens to induce identical effector functions.

Antigen
Variable region
Constant region

IMMUNITY

IMMUNITY

IMMUNITY

Different variable regions bind different antigens. Identical constant regions

induce identical responses. e.g. same class of Ig for different m.organisms.

BINDING OF ANTIGEN BY ANTIBODY - TERMS AND CONCEPTS

Antibodies bind antigens by reversible noncovalent interactions. formed by a combination

Epitope

of hydrogen bonds, hydrophobic interactions,

electrostatic and van der Waals forces.

Epitope

Epitope: The parts of an antigen recognized

by an antibody are called epitopes. Epitopes
can be recognized on the basis of sequence
or shape.

Affinity: is the strength of the reaction between a

single antigenic determinant and a single
combining site on the antibody.

What is
paratope ?

Avidity: Indicates the overall strength of : antigen antibody complex.

Influenced by 3 parameters:
Ka ( affinity constant).
The valency of (both antigen & antibody).
Structural arrangement of the parts that interact.

Specific Antibody (Ig) Molecules Are Tailored to Exactly Fit A

3 D Surface Site On An Antigen.
Epitope

Paratope

IMMUNOGLOBULIN ISOTYPES
There are five types of heavy chain that differ in
their C region. Each class is known as an
Isotype.
Each Isotype differs in their physical/biological
properties and effector functions.

Why passive ?
IgA. Two IgA
molecules joined
by J chain.

The J chain facilitates transport of IgA

across mucosal epithelia. The J chain
also facilitates transfer of IgA to
newborns to confer neonatal passive
immunity.

IMMUNOGLOBULIN ISOTYPES

IgD. Function unknown.

Restricted to membrane and not expressed on
active B lymphocytes.
IgD knock-out mice do not have any apparent
defects.
Seen on the surface of nave B cells.

IMMUNOGLOBULIN ISOTYPES
Antigen

IgE

Secreted as a
monomer.

Fc Receptor

MAST
CELL

IgE binds the Fc receptors of mast cells.

When IgE is cross-linked by

antigen, it triggers mast cell
degranulation - allergic
response.

IMMUNOGLOBULIN ISOTYPES
Secreted as
monomer

IgG can bind

and neutralize
toxins.

IMMUNOGLOBULIN ISOTYPES
Opsonization: IgG coats pathogens and
prevents them from entering host cells.

Infectious pathogen
entering host cell
to propagate

Pathogen cannot
enter cell
when coated
(opsonized) with
antibody

Ag
IgG

Antibody mediated Phagocytosis

FcR

Phagolysosome

Macrophage

MHC II/peptide

1. IgG-Ag binds the Fc receptor of

macrophages.
2. Ag is internalized through phagocytosis.
3. Microbe is degraded in the phagolysosome.
4. Microbial peptides are presented on Class II
MHC molecules - CD4 T cell activation!

IMMUNOGLOBULIN ISOTYPES
Fc receptors also mediate Antibody-Dependent
Cellular Cytotoxicity (ADCC)
Natural Killer Cells

Ig

Target

Ag

1. Ig binds Ag on surface of target cell.

2. Fc Receptors on Natural Killer cells bind Fc
of Ig.
3. Cross-linking of Fc receptors signals to the
NK cell to kill the target.

Cell Lysis &

Apoptosis ?

4. Target cell dies by apoptosis perforin & granzymes

IMMUNOGLOBULIN ISOTYPES
IgM exists as pentamers
10 different Ag binding
sites - very high avidity!

As with IgA, it has a J

chain for secretion.
IgM is the first antibody expressed in mature B
cells.
Important for activation of the complement
pathway. Appears early after infection and
usually not seen upon re-infection.