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Antibodies

All about Antibodies

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24 views15 pages

Antibodies

All about Antibodies

Uploaded by

abhi.aryanyp
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Antibodies

Dr. Charu Tripathi


Assistant Professor
CMP College (University of Allahabad)
Antibodies
• Antibodies are the antigen-binding proteins present on B-cell
membrane and secreted by plasma cells.

• Secreted antibodies circulate in the blood, where they serve as the


effectors of humoral immunity by searching out and neutralizing
antigens or marking them for elimination.
Epitopes or Antigenic Determinants
• Epitopes are immunologically active regions of an
immunogen that bind to antigen-specific
antibodies.
• Most antigens contain many different epitopes,
therefore they lead to the activation of several
different B-clones. Such serum containing
antibodies specific to different epitopes is known as
polyclonal serum.
Structure of Antibodies
• There are 4 polypeptide chains: 2 identical
light (L) chains of 22 kDa and 2 identical
heavy (H) chains of 55 kDa.
• Light chains are bound to heavy chains by
disulfide bonds.
• They have two regions: a constant region and
a variable region.
• Antibodies are glycoproteins, therefore there
are some carbohydrate moieties attached at
the constant region.
Constant region
• CL in the light chain and
• CH in the heavy chain.
Variable region
• First ~100 amino acids of the amino terminal
of L and H chains (VL in the light chain and
VH in the heavy chain) comprise the variable
region.
• This region determines the specificity of the
antibody.
• Areas within the variable region responsible
for imparting specificity are called CDRs
(complementarity determining regions).
• CDRs comprise the antigen binding site of
the antibody.
Enzymatic digestion of IgG
• Digestion of IgG with papain yields 3
fragments: 2 fragments of Fab (fragment
antigen binding) and 1 fragment of Fc
(fragment, crystallizable).
• Digestion of IgG with pepsin yields 2 Fab
like units called F(ab’)2 fragment. In this
digestion, Fc fragment is not recovered as
it has been digested into smaller
fragments.
• Treatment with mercaptoethanol reduces
the disulphide bonds and yields 2 heavy
chains and 2 light chains.
Light chains
• Variable (V) and constant (C) regions.
• Constant region has two types of chains:
either kappa (κ) or lambda (λ).
• In humans, ~60% light chains are kappa,
40% are lambda.
• However in mice, 95% chains are kappa
and only 5% are lambda.
• An antibody contains either κ or λ, never
both.
Heavy chains
• Variable (V) and constant (C) region.
• Constant regions are of 5 types: μ, δ, γ, ε, and
α.
• δ, γ and α have ~330 amino acids.
• μ and ε have ~440 amino acids.
• Heavy chain types determine the antibody
class:
• IgM (μ)
• IgG (γ)
• IgA (α)
• IgD (δ)
• IgE (ε)
Immunoglobulin G (IgG)
• Most abundant – 80% of total serum immunoglobulin.
• It has two γ heavy chains and two κ or λ light chains.
• IgG is of 4 types: IgG1, IgG2, IgG3, and IgG4.
• It can readily pass the placenta, playing an important role in the
protection of fetus.
• IgG3 is the most effective complement activator.
• They bind to Fc receptor on phagocytic cells, mediating opsonization
(promotion of phagocytosis of antigens by macrophages and
neutrophils).
Immunoglobulin M (IgM)
• Present ~5% - 10% of total serum immunoglobulin.
• Monomeric IgM is expressed as membrane bound antibody
on B cells.
• Secreted IgM is produced by plasma cells. It is a pentamer
linked by disulfide bonds.
• Fc regions are in the center in the pentamer and 10 antigen
binding sites are towards the periphery.
• Pentamer contains an extra Fc polypeptide called J (joining)
chain.
• IgM is the first Ab to be produced during immune response
and also the first to be synthesized by a neonate.
• Activates complement more efficiently than IgG.
• More efficient in causing agglutination as it is a pentamer.
• It is present in external secretions, such as mucosal
secretions (but less than IgA).
Immunoglobulin A (IgA)
• Present ~10-15% of total immunoglobulin in serum.
• Predominant Ig class in external secretions like milk,
saliva, tears and mucus.
• Secretory IgA is mostly a dimer or tetramer having J-
chain.
Immunoglobulin E (IgE)
• It has low serum concentration.
• Mediate hypersensitivity reactions responsible for
hay fever, asthma, hives and anaphylactic shock.
• IgE binds to Fc receptors on the membranes of
basophils and tissue mast cells which then release
histamines and other substances that mediate allergic
reactions (degranulation).
Immunoglobulin D (IgD)
• Constitutes 0.2% of total immunoglobulins in serum.
• IgD and IgM are major membrane – bound immunoglobulins
expressed by mature B cells.
• Its exact functions are not very clear.
Thank You

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