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1. KOMAL FATIMA
ROLL#5
MPHIL.ZOOLOGY (1ST )
COURSE TITLE:
IMMUNOLOGY
COURSE INSTRUCTOR:
DR.SAMRAH MASUD
Presentantation :immunoglobulin (IGE)

2. PRESENTATION TOPIC
• Immunoglobulin
• IgE

3. IMMUNOGLOBULIN
Immunoglobulin is a
glycoprotein that is made in
response to an antigen and can
recognize and bind to an
antigen that caused it’s
production

4. IMMUNOGLOBULIN
• Immunoglobulin E(IgE)
• Definition :
• It is a type of antibody( or immunoglobulin (Ig)
“isotype” that has been found only in mammals

5. DISCOVERY
• IgE was simultaneously discovered in 1966 and 1968
• It was discovered by two independent groups Kimishige
ishizaka and his wife Teruko ishizaka at Children’s Asthama
Research institute and Hospital in Denver.
• Their joint paper was published in April 1969

6. STRUCTURE
• IgE is synthesized by plasma cells
• Monomers of IgE consists of two heavy chains epsilon (e) and
two light chains
• (e ) chain containing four Ig- like constant domains (CE1-CE4)
• Both light chains and heavy chains linked by numerous
intrachain di sulphide bonds
• IgE is found similar to IgG in structure but IgE has two uniques
features

8. UNIQUE FEATURES
• The epsilon (e) heavy chains consists of high carbohydrate
content (12%)
• Additional constant region (CH4)
• The structure has two identical antigen binding areas
consisting of both light chains (23KDa) and heavy chains
70KDa).
• Disulphide links that divide each chain into areas called as
“domains”

9. DIFFERENCE BETWEEN LIGHT CHAINS AND
HEAVY CHAINS
• Light chains
• It has two domains
• One constant
• One variable
• Heavy chains
• It has five domains
• One variable
• Four constant region domains (
additional constant region (CH4)

10. N TERMINI AND C- TERMINAL REGIONS
• Both heavy and light chains have their variable region on their most N-
terminal ends
• Variable (v) sequences at the N- termini of the heavy (VH) and light (VL)
chains create unique antigen binding specific sites.
• C terminal regions of heavy chains are made up of 4 Ce domains
• The unique CH4 region restricts IgE binding to high – affinity receptors
(Fce-R1) on the surface of basophils and mast cells which contains granules
of heparin and histamine
• A hinge region is absent in the structure of IgE
• IgE antibodies are heavily glycosylated required for its binding to high –
affinity receptors

12. FUNCTIONS
• IgE provides protection against
helminth parasites
• Respond to foreign substances acts
as “gatekeeper”
• IgE function as mediators in allergic
reactions in allergic reactions Type I
• Interact with both antigen and
receptor molecules on surface of
blood basophils and tissue mast
cells in human body
• Innitiates release of histamine and
heparin

13. • IgE has essential role in type l hypersensitivity which menifests in
assorted allergic reactions
1. Food allergies
2. Allergic Asthama
3. Sinusitis
4. Allergic rhinitis ( hay fever)
• High level of IgE indicate that body is overreacting to allergens
leading to allergic reactions

14. IMMUNE RESPONSE TO PARASITES
• IgE plays role in immune response to parasites such as Shistosoma
mansoni,Fasciola hepatica
• IgE is utilized during immune defense against certain protozoans
parasites such as Plasmodium falciparum
• Release of histamine contribute in expulsion of parasites
• IgE point to certain clues such as risk of allergies , infections and
some chronic diseases
• IgE blood test (an allergic person produces specific IgE antibodies)