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IMMUNOGLOBULINS Structure, function and types IMMUNOGLOBULINS Structure, function and types

IMMUNOGLOBULINS Structure, function and types - PowerPoint Presentation

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IMMUNOGLOBULINS Structure, function and types - PPT Presentation

Dr Vinod KV Also known as antibodies They are glycoproteins produced by the body against antigenic stimulus Synthesised by B lymphocytes Basic structure Igs are glycoproteins Made up of two pairs of polypeptide chains ID: 934500

region amp chain chains amp region chains chain variable constant serum regions cells provide binding days monomer responsible life

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Slide1

IMMUNOGLOBULINS

Structure, function and types

Dr.

Vinod

K.V.

Slide2

Also known as antibodiesThey are

glycoproteins produced by the body against antigenic stimulus

Synthesised by B lymphocytes

Slide3

Slide4

Basic structure

Igs are

glycoproteins

Made up of two pairs of polypeptide chains

One pair light chains- L chains (mw 25000

da

)

One pair heavy chains-H chains (50000

da

)

L & H chain and H & H chains are joined by disulphide bond

4 chains are joined to form a flexible Y shaped molecule

Slide5

Slide6

Two regions-

Fab region &

Fc

region

Fab

region- at the tip of each arm of Y

Fc

region- limited in variability, responsible for the biological activity, act as receptor binding portion (to

phagocytic

cells), bind to complement

Ag binding site @ amino terminus

Ag binding site composed of both H & L chains

Slide7

Both chains composed of two portions- variable region (N) & constant regions (C)

Constant region – constant sequence- One constant domain in L chain (C

L

) & 3-4 domains in H chain (C

H1

, C

H2

, C

H3

)

Variable region – one domain in both H & L chains- highly variable & determines immunological specificity

Hyper variable regions (hot spots)- highly variable region in the variable regions

Slide8

Slide9

Intra chain S-S bonds form loops form globular domains

VL & VH are responsible for Ag binding site

Hinge region- between CH1 & CH2 , flexible and more exposed to enzymes & chemicals

Slide10

Slide11

Slide12

L chains are of two types- Kappa & lambda (2:1 ratio in human sera)

H chain 5 types- A, D, G, E & M

Slide13

ANTIBODY STRUCTURE

Antigen

Variable region

Constant region

IMMUNITY

IMMUNITY

IMMUNITY

Different variable regions bind different antigens. Identical constant regions induce identical responses.

Slide14

Classes of immunoglobulins

IgG

heavy chain is gamma

most common & major serum

Ig

(75-80%)

Circulating

Ig

equally distributed in intra & extra vascular compartments

Contains less CHO than other

Igs

mw 1,50, 000

da

, half life 23 days

8-16 mg/100 ml serum concentration

Exist as monomer

Only

Ab

that can cross placenta & provide natural passive immunitySecondary response Ab- second exposure- production of Ig G is very rapid

Slide15

provide long term resistance

4 sub classes- Ig G1-IgG4

Functions

General purpose

Ab

, protective against agents in blood & tissues

Enhance

phagocytosis

Participate in most immunological reactions

neutralise toxins in blood & tissues

Best for opsonisation

Cross placenta

Slide16

Ig

A

Second most abundant (10-13%)

mw 4,00,000

da

half life 6-8 days

Major

Ig

in

colostrum

, tear & saliva

Low in serum (0.6-4.2 mg/100ml)

Two forms- monomer (in serum) &

dimer

(in secretions called

secretory

Ig

A)Synthesised by plasma cells near mucosaHas a secretory piece produced by mucosa helps to cross mucos membrane & prevent from denaturation

J chain connect monomersSub classes- Ig A1 & Ig A2

Slide17

Functions

Secretory Ig

A provide protection to respiratory & gastrointestinal tracts by inhibiting the attachment of the microbes to mucosa

Causes

degranulation

of

eosinophils

&

basophils

Enhance

phagocytosis

by

monocytes

Activate alternate pathway

weak in opsonisation

Slide18

Ig

M

Third common

Ig

(5-8%)

occurs as a

pentamer

(J chain)- largest

Ig

First

Ig

to appear in circulation- Primary response

First

Ab

to be formed in

fetus

Deficiency is associated with

septicemia

Ig M is short lived, hence its presence indicate recent infectionFour constant domains500-1000 times more effective than Ig G in opsonisation, 100 times in bacterial action, 20 times in bacterial agglutination

Neutralisation is less effective

Slide19

Function

Detection is useful in the diagnosis of syphilis, HIV, Dengue fever..Good at complement fixationCauses

lysis

of microbes

Effective in attaching to surface antigenic determinants

Responsible for protection against blood invasion by microbes

Slide20

Ig D

Resembles

Ig

G in structure

Monomer

Mostly intravascular (3mg/100ml)

Half life 3 days

Occurs on the surface of

unstimulated

B cells

Cell Bound

Ig

D are k type, serum

Ig

D are L type

Slide21

Functions

Helps in Ag recognition by B cellsBinding of cell bound Ig

D with Ag leads to stimulation of B cells, activation or cloning to produce

Ab

Slide22

Ig

E

Resembles

Ig

G structurally

Monomer

Found only in mammals

mw 1,90,000

da

half life 2 days

Extravascular

Ig

Normal serum level in traces but elevated in allergic conditions

Affinity to surface of mast cells-helps to produce histamines

Mainly produced in the lining of respiratory & intestinal tracts

Slide23

Function

Provide protection by being hypersensitiveCauses inflammatory responseSpecial role in defence against

helminth

infection

responsible for allergic reactions