Immunochemistry imc 02
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Transcript of Immunochemistry imc 02
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IMMUNOCHEMISTRYANTIGENS
ANTIBODIES
Dr. Aga Syed SameerCSIR Lecturer (Demonstrator)
Department of Biochemistry,
Medical College,
Sher-I-Kashmir Institute of Medical Sciences,
Bemina, Srinagar, Kashmir, 190018. India.
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Antigens
Substances that can be recognized by the immunoglobulin receptor of B cells, or by the T cell receptor when complexedwith MHC, are called antigens.
Although a substance that induces a specific immune response is usually called an antigen, it is more appropriately called an immunogen.
Antigenicity is the ability to combine specifically with the final products of the above responses (i.e., antibodies and/or cell-surface receptors). Although all molecules that have the property of immunogenicity also have the property of antigenicity, the reverse is not true.
Hapten: Small foreign molecule that is not antigenic. Must be coupled to a carrier molecule to be antigenic. Once antibodies are formed they will recognize hapten. It is antigenic but not immunogenic.
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Antigens
Immunogenicity of Antigen is determined, in
part, by four properties:
Its foreignness,
Molecular size,
Chemical composition and complexity, and
Susceptibility to antigen- processing & presentation
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Antigens
Foreignness
When an antigen is introduced into an organism,
the degree of its immunogenicity depends on the
degree of its foreignness.
Generally, the greater the phylogenetic distance
between two species, the greater the structural
(and therefore the antigenic) disparity between
them.
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Antigens
Molecular Size
The most active immunogens tend to have a
molecular mass of 100,000 daltons (Da).
Generally, substances with a molecular mass
less than 5000–10,000 Da are poor
immunogens.
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Antigens
Complexity & Composition
Size and foreignness are not, by themselves,
sufficient to make a molecule immunogenic;
other properties are needed as well.
In this regard it is notable that all four levels of
protein organization—primary, secondary,
tertiary, and quaternary—contribute to the
structural complexity of a protein and hence
affect its immunogenicity.
Copolymers composed of different amino acids
or sugars are usually more immunogenic than
homopolymers of their constituents.
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Antigens
Susceptibility to Antigen- Processing and
Presentation
Large, insoluble macromolecules generally
are more immunogenic than small, soluble
ones because the larger molecules are more
readily phagocytosed and processed.
Macromolecules that cannot be degraded and
presented with MHC molecules are poor
immunogens.
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Antigens – In Generality
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.
Molecular weight of 10,000 or higher.
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Adjuvants
Adjuvants (Latin: adjuvare, to help) are substances that, when mixed with an antigen and injected with it, enhance the immunogenicity of that antigen.
Adjuvants are often used to boost the immune response when an antigen has low immunogenicity or when only small amounts of an antigen are available. Bovine Serum Albumin
Alum
Freund’s (in)complete adjuvant
Bacterial lipopolysaccharide
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ANTIGENS
Epitope or Antigenic Determinants:
Immunologically active regions of an Antigen that
bind to antigen-specific membrane receptors on
lymphocytes or to secreted antibodies.
Small part of an antigen that interacts with an
antibody.
Any given antigen may have several epitopes.
Each epitope is recognized by a different antibody.
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EPITOPES: ANTIGEN REGIONS THAT
INTERACT WITH ANTIBODIES
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IMMUNOGLOBULINS: STRUCTURE AND
FUNCTION
Glycoprotein molecules that are produced by plasma cells in response to an immunogen and which function as antibodies
Immune serum
Ag adsorbed serum
+ -
albumin
globulins
Mobility
Am
ou
nt
of
pro
tein
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Fab
Ag binding
Fc
Effector functions
F(ab’)2
Pepsin
Fc
Peptides
F(ab’)2
IMMUNOGLOBULIN FRAGMENTS:
STRUCTURE
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IMMUNOGLOBULIN FRAGMENTS:
STRUCTURE
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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.
IMMUNOGLOBULIN STRUCTURE
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Variable & Constant
Regions
VL & CL
VH & CH
Hinge Region
CH1
VL
CL
VH
CH2 CH3
Hinge Region
Carbohydrate
Disulfide bond
IMMUNOGLOBULIN STRUCTURE
The four chains are linked by disulfide bonds.
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L chains are one of two types:
Designated κ and λ
Only one type is found in particular Ig
H chains are distinct for each of the five Ig
classes or isotypes:
Designated γ, α, μ, δ, ε for the respective classes of
Ig: IgG, IgA, IgM, IgD & IgE.
IMMUNOGLOBULIN STRUCTURE
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IMMUNOGLOBULIN STRUCTURE
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MYELOMA ??
A myeloma cell is a cancerous plasma cell
Its protein-synthesizing machinery and secretory
functions are not altered
These Plasma Cells continue to secrete
molecularly homogeneous antibodies
These antibodies are similar to normal antibodies
but because of their source they are represented as
myeloma proteins
Myeloma protein can account for 95% of the serum Igs
Bence-Jones proteins represent the light chains of Igs that
make their way in the urine of such patient
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Immunoglobulins
Structure
Function
Secretion
NEXT LECTURE:
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QUESTIONS?