2. Antigen
Any substance which ,when introduced
parentrally into the body, stimulates
the production of antibody with which
it reacts specifically & in observable
manner.
Either humoral or cell mediated
immunity
3.
4. Specificity – Ag introduced in body
react with those particular
immunocytes which carry specific
marker for that antigen
Ab produced will react with that
particular Ag
5. Epitope
Smallest unit of antigenicity, antigenic
determinant
Small area on Ag capable of combining
complementary site on Ab or T
lymphocyte.
9. Most are proteins or large polysaccharides from
a foreign organism.
– Microbes: Capsules, cell walls, toxins, viral
capsids, flagella, etc.
– Nonmicrobes: Pollen, egg white , red blood
cell surface molecules, serum proteins, and
surface molecules from transplanted tissue.
Lipids and nucleic acids are only antigenic
when combined with proteins or
polysaccharides.
10. Antibody
Proteins that recognize and bind to a particular
antigen with very high specificity.
Made in response to exposure to the antigen.
One virus or microbe may have several
antigenic determinant sites, to which different
antibodies may bind.
Each antibody has at least two identical sites
that bind antigen: Antigen binding sites.
Valency of an antibody: Number of antigen
binding sites. Most are bivalent.
Belong to a group of serum proteins called
immunoglobulins (Igs).
11. Function of Ab
Elimination of foreign antigen
Recruitment& enhancement of host
effector mechanism
antibody levels in diagnosis
Passive administration -therapy
15. Antibody structure
Monomer: A flexible Y-shaped molecule with
four protein chains:
– 2 identical light chains
– 2 identical heavy chains
Variable Regions: Two sections at the end of Y’s
arms. Contain the antigen binding sites (Fab).
Identical on the same antibody, but vary from
one antibody to another.
Constant Regions: Stem of monomer and lower
parts of Y arms.
Fc region: Stem of monomer only. Important
because they can bind to complement or cells.
16. Lock and Key Concept
concept of antigen-antibody reactions
is one of a key (i.e. the antigen) which
fits into a lock (i.e. the antibody).
Ab
Ag
18. Immunoglobulin –proteins of
animal origin
Chemically antibodies are
globulines and hence they are
called as immunoglobulines
Synthesised by plasma cells & B
lymphocytes
All antibodies are Ig. But not true
vice-versa
21. IgG
Structure: Monomer
Percentage serum antibodies:
80%Most common
Location: Blood(12mg/ml), lymph, intestine
Molecular weight150 kDa
Half-life in serum: 23 days
22. IgG
Complement Fixation, Neutralisation,
precipitation : Yes
Diffuses easily IV & EV compartments
Placental Transfer: Yes
Known Functions: Enhances
phagocytosis, neutralizes toxins and
viruses, protects fetus and newborn.
23. IgG
Catabolic rate depends directly on
conc. Of IgG.
Passive immunisation suppresses
homologus Ab producion used in
Anti RhiD isoimmunisation
IgG1, IgG2,IgG3,IgG4
IgG1, IgG3 activators of classical
complement pathway
25. IgM
Structure: Pentamer
Percentage serum antibodies: 5-10%
Location: Blood(0.5-2mg/100ml), lymph, B
cell surface (monomer)
Half-life in serum: 5 days
Complement Fixation: Yes
Placental Transfer: No
Known Functions: First antibodies
produced during an infection. Effective
against microbes and agglutinating
antigens.
26. Pentamer, 5 H & L chains, One
molecule of J Chain
Can not spread from blood to
tissues
27. Functions of IgM
Protection against bacteraemia
Pramotes phagocytosis &
bacteriolysis by complement
activation
Primary immune response
infection
Can not cross placenta- presence
in new borne IU infection
Major component of rheumatoid
factor
30. IgA
Structure: Dimer
Percentage serum antibodies: 10-15%
Location: Secretions (tears, saliva,
intestine, milk), blood and lymph.
Half-life in serum: 6 days
Complement Fixation: No
Placental Transfer: No
Known Functions: Localized protection of
mucosal surfaces. Provides immunity to
infant digestive tract.
31. Serum IgA & Secretory IgA
Covers microorganisms and
prevents adhesion to mucosal
surface
33. IgD
Structure: Monomer
Percentage serum antibodies: 0.2%
Location: B-cell surface, blood, and lymph
Half-life in serum: 3 days
Complement Fixation: No
Placental Transfer: No
Known Functions: In serum function is
unknown. On B cell surface, initiate
immune response.
35. IgE
Structure: Monomer
Percentage serum antibodies:
0.002%
Location: Bound to mast cells and
basophils throughout body. Blood.
Half-life in serum: 2 days
Complement Fixation: No
Placental Transfer: No
Known Functions: Allergic reactions.
Possibly lysis of worms.
36. It is mostly distributed in
extravascular space.
IgE + mast cell serves as receptor
for allergens and parasitic antigens
Mast cells degranulated with
release of vasoactive amines
Increased IgE parasitic infection
38. Multiple myeloma
Plasma cell tumor in bone marrow
Producing excess of single class
of immunoglobulin (M proteins)
All 5 classes
Myeloma with IgM producing cells
is called as Waldenstrom’s
macroglobulinemia
39. Bence Jones protein
Light chains of immunoglobulins
Present in urine of myeloma
patients
Either kappa or lambda
Coagulates when heated at 600
C
redisolves at 800
C
40. Cryoglobulinaemia
Presence of cryoglobulin in blood
Precipitate in microvasculature on
exposure to cold
Associated with SLE, myeloma,
macroglobulinaemia.
Made up of IgG, IgM or mixture