ACQUIRED

IMMUNITY
by

Dr John Shia
What is Acquired Immunity?
• Acquired immunity (specific) is developed through the contact
with disease agent, vaccination, or via passive antibody transfer.

• Innate immunity (non-specific) refers to the natural resistance

when a person is born.

- Antibodies in milk

- Natural infection

- Venom antiserum

- Vaccination
The History of Acquired Immunity
• It has been long recognised that people who did not die
from a certain life-threatening disease (e.g. smallpox) were
subsequently more resistant to that disease than those
who had never been exposed to it.

• The validation was carried out by Dr. Edward Jenner

(1749-1823), the father of immunology.

• He is also the pioneer of smallpox vaccine, the world’s first

vaccine.
• Dr. Edward Jenner inoculated a young boy (his
gardener’s son) with pus from the blister of a dairy
maid who had cowpox, a relatively benign disease
that is related to smallpox.

• He then deliberately exposed the boy to smallpox.

• This exposure failed to cause disease because of the

protective effect of cowpox inoculation.
• Because of this incidence, the process of inducing acquired
immunity has been termed vaccination.
(Vaccinia, from the Latin word, means “cow”)

• If he were to perform his experiment today, his medical license

would have been revoked under malpractice.

Lesions on
human’s arm
Pus at
Cow’s teats
ANTIGENS &
ANTIBODIES

By
Dr John Shia
Antigen/ Immunogen
• An antigen (Ag) is a molecule or molecular structure, present on the outside of
a pathogen.

• It can be bound by an antigen-specific antibody or B-cell antigen receptor.

• Antigen stands for antibody generator. Its presence in the body normally triggers
an immune response.

• Antigens are "targeted" by specific antibodies. Each antibody is specifically

produced by host’s immune system to match an invading antigen.

• In most cases, an antibody can only react and bind to a specific antigen; in some
instances, however, antibodies may cross-react and bind more than one antigen
(molecular mimicry).
Four Sources of Antigens
1. Exogenous antigens. These antigens enter the body from the outside, for
example, by inhalation, ingestion or injection. e.g. Pollen, chemicals, pathogens.

2. Endogenous antigens. These antigens are generated within normal cells as a

result of normal cell metabolism, or because of viral or intracellular
bacterial infection.

3. Autoantigen. This is usually a self-protein or protein complex (and sometimes DNA

or RNA) that is recognised by the host’s immune system as foreign, commonly seen
in autoimmune diseases.

4. Neoantigens. Neoantigens are those that are entirely absent from the normal
human genome. e.g tumour antigens
Hapten
• Hapten is an antigen with the molecular weight (MW) < 1KDa. Somehow it lacks
antigenicity on its own.

• However, once attached to a larger carrier protein, it elicits an immune response.

• The carrier may be one that does not elicit an immune response by itself. E.g.
penicillin-induced hypersensitivity.
What is the fate of antigen after penetration?
Antibody
By
Dr John Shia
Structure of an Antibody/Immunoglobulin
• It consists of heavy and light chains. Each chain has a VL- Variable
constant and a variable region. region for light
chain.

CL- constant
region for light
chain.

VH- Variable
region for heavy
chain.

CH- Constant
region for heavy
chain.
• When digested with pepsin or papain (protease), antibody
breaks into two fragments:
i) Fab (antigen binding fragment)
ii) Fc (crystalisable fragment)

• The immunoglobulin specificity, as well as its capability to

react with the antigen, are determined by the paratope at
Fab.

• The effector role is performed by the Fc; activating

complement system, or binding to the cell receptors.
Five (5) Classes of Immunoglobulin
• Constant domain determines the type of immunoglobulin; IgM,
IgG, IgA, IgE, and IgD.

• Structurally, they are either pentamer, dimer, or monomer.

1.Biological Properties of IgG
• IgG has a half-life of 23 days (catabolism rate).

• Its persistence in serum makes IgG the most

suitable candidate for passive immunisation (direct
transfer of antibodies).

• IgG is the only class of immunoglobulin that passes

through the placenta.
Functions of IgG
1. IgG immobilises pathogens via agglutination. It coats the surface of pathogen,
(opsonisation process), allowing their recognition and ingestion by phagocytes.

2. IgG activates classical pathway of the complement system that results in

pathogen elimination.

3. IgG binds and neutralises toxins.

4. IgG also plays an important role in antibody-dependent cell-mediated

cytotoxicity (ADCC) and intracellular antibody-mediated proteolysis. It binds
to TRIM21 (Tripartite motif containing-21, an IgG receptor) in order to prevent
further viral replication

5. IgG is also associated with type II and type III hypersensitivity reactions.
 Antigen

Antibodies
Antibody
FC receptor

FC receptor

• In antibody-dependent cell-mediated
cytotoxicity (ADCC), Fab binds to tumour cell
• In opsonization, antigen-IgG or microorganism, while its Fc portion binds to
complexes are more readily bound the Fc receptor of Natural Killer cells.
to the FC receptors of phagocytes.
• NK cell then releases perforin and granzymes to
destroy the target cells.
• IgG molecule is an excellent antibody for the neutralisation of
toxins such as tetanus and botulinus, and for the inactivation
of snake and scorpion venoms (passive immunisation). Neutralisation
by antibody

• It neutralises such toxins/venoms by blocking their active sites.

2. Biological Properties of IgM
• The half-life is approximately 5 days.

• IgM antibodies are poor neutralising

antibodies for toxins and viruses.

• Because of its pentameric form, IgM is an

excellent complement-fixing antibody.

• IgM antibodies DO NOT pass through the

placenta.

• Since IgM is the only class of immunoglobulin produced by the

fetus (5th month onwards), elevated level of IgM indicates
congenital or perinatal infection.
3. Biological Properties of IgA
• Most IgAs are present in secretions such as tears, saliva, sweat, mucus,
and breast milk.

• Approximately 3-5 grams of IgA (15% of total Ig produced) are secreted

into the intestinal lumen daily. It prevents the attachment of organisms to
the epithelial surface.

• IgA is NOT a complement-activating

immunoglobulin (no receptor for
complement).
4. Biological Properties of IgD
• IgD functions mainly as an antigen receptor on B
cells that have not been exposed to antigens.

• It has been shown to activate basophils and mast

cells to produce antimicrobial factors.

• In mature B cells, IgD co-expresses with IgM to

serve as an antigen-binding surface.
 5. Biological Properties of IgE
• It has a half-life of 2 days in serum, the shortest of all
classes of immunoglobulins.

• Once bound to mast cells and basophils, IgE may be

retained by these cells for weeks or months.

• When antigen appears, it creates cross-linking of IgE

molecules.

• This activates the mast cells and basophils to release

histamine, heparin, and leukotrienes.
• The reaction may be mild, as in the case of a
mosquito bite, or severe, as in the case of
bronchial asthma; or may even result in
systemic anaphylaxis, which leads to death
within minutes.

• IgE is not a complement-activating antibody. The

protective effect is achieved by activation of acute
inflammatory response.

• Elevated IgE in serum have been shown to occur

during infections with ascaris (roundworm).
Antibody Isotypes not Found in Mammals
• IgY- Found in birds and reptiles; related to mammalian IgG.

• IgW- Found in sharks and skates (similar to stingray); related

to mammalian IgD.
THANK YOU!