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Antibody
Dr. Rupali Mali
MBBS,MD (Microbiology)
Lecturer , Department of Microbiology
SKNMC & GH
Narhe, Pune.
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
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
Epitope
Smallest unit of antigenicity, antigenic
determinant
Small area on Ag capable of combining
complementary site on Ab or T
lymphocyte.
Paratope
Corresponding area on antibody which
combines with epitope is called as
paratope.
Epitope
Determinants of antigenicity
Size of Ag
Chemical nature of Ag
Susceptibility to tissue enzymes
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.
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).
Function of Ab
Elimination of foreign antigen
Recruitment& enhancement of host
effector mechanism
 antibody levels in diagnosis
Passive administration -therapy
Antibody structure
Papain digestion
Pepsin digestion
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.
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
Types of Abs or Immunoglobulines
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
Types of Ig
IgG (Gammaglobulin)
IgM (Mu)
IgD (Delta)
IgE (Epsilon)
IgA (Alpha)
IgG -Monomer
IgG
Structure: Monomer
Percentage serum antibodies:
80%Most common
Location: Blood(12mg/ml), lymph, intestine
Molecular weight150 kDa
Half-life in serum: 23 days
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.
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
IgM -pentamer
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.
Pentamer, 5 H & L chains, One
molecule of J Chain
Can not spread from blood to
tissues
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
Agglutination,Complement fixation,
cytolytic actions.
IgA -Dimer
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.
Serum IgA & Secretory IgA
Covers microorganisms and
prevents adhesion to mucosal
surface
IgD - Monomer
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.
IgE – attaches to basophil
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.
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
Abnormal immunoglobulines
Bence Jones protein – multiple
myelome
Waldenstrom’s macroglobulinemia
– myeloma, IgM producing cell
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
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
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

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Antigen and antibdy

  • 1. Antibody Dr. Rupali Mali MBBS,MD (Microbiology) Lecturer , Department of Microbiology SKNMC & GH Narhe, Pune.
  • 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.
  • 6. Paratope Corresponding area on antibody which combines with epitope is called as paratope.
  • 8. Determinants of antigenicity Size of Ag Chemical nature of Ag Susceptibility to tissue enzymes
  • 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
  • 17. Types of Abs or Immunoglobulines
  • 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
  • 19. Types of Ig IgG (Gammaglobulin) IgM (Mu) IgD (Delta) IgE (Epsilon) IgA (Alpha)
  • 21. IgG Structure: Monomer Percentage serum antibodies: 80%Most common Location: Blood(12mg/ml), lymph, intestine Molecular weight150 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.
  • 34. IgE – attaches to basophil
  • 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
  • 37. Abnormal immunoglobulines Bence Jones protein – multiple myelome Waldenstrom’s macroglobulinemia – myeloma, IgM producing cell
  • 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