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Antibodies Structure and Function

1. Antibodies, also known as immunoglobulins, are glycoprotein molecules produced by plasma cells that function to recognize and bind to foreign objects in the body called antigens. 2. Antibodies have two regions - the Fab region that determines antigen specificity and the Fc region that determines the effector functions once binding occurs. 3. There are five major classes of antibodies (IgG, IgA, IgM, IgE, IgD) that have different structures and functions such as neutralization, opsonization, complement activation, and activation of cellular elements.

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ياسين احمد علي الشيخ
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519 views

Antibodies Structure and Function

1. Antibodies, also known as immunoglobulins, are glycoprotein molecules produced by plasma cells that function to recognize and bind to foreign objects in the body called antigens. 2. Antibodies have two regions - the Fab region that determines antigen specificity and the Fc region that determines the effector functions once binding occurs. 3. There are five major classes of antibodies (IgG, IgA, IgM, IgE, IgD) that have different structures and functions such as neutralization, opsonization, complement activation, and activation of cellular elements.

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ياسين احمد علي الشيخ
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© © All Rights Reserved
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ANTIBODIES: STRUCTURE

AND FUNCTION
2
Dr. Taha Abdul-Aziz saeid kaid
Assistant professor of
Microbiology and Medical Immunology

770489955-‫مكتبة العامرية للخدمات الطالبية المتكاملة ت‬


Immunoglobulins
• Immunoglobulins (Ig): are glycoprotein molecules which are produced by
plasma cells in response to an immunogen and which function as antibodies.
The immunoglobulins derive their name from the finding that when
antibody-containing serum is place in an electrical field the antibodies, which
were responsible for immunity, migrated with the globular proteins.
• Two broad actions,
1. Antigen Recognition
2. Outcome Determination
• these functions are sub served by different
regions of the immunoglobulin moiety,
1. Fraction Antigen Binding Fab
this is the highly variable area which determines specificity
2. Fraction Crystalline Fc
which determines what happens once the Ab-Ag interaction has occurred
Serum proteins electrophoresis in diagnostics
of diseases
Normal pattern
Reference ranges:

Total protein 6.0 – 8.0 g/dL


Albumin 3.5 – 5.0 g/dL
α1-globulins 0.1 – 0.4 g/dL
α2-globulins 0.4 – 1.3 g/dL
β-globulins 0.6 – 1.3 g/dL
γ-globulins 0.6 – 1.5 g/dL

Figure is found at http://erl.pathology.iupui.edu/LABMED/INDEX.HTM


Antibody Structure
• Antibodies Are Made Up Of:
– 2 Light Chains (identical) ~25 KDa
– 2 Heavy Chains (identical) ~50 KDa
• Each Light Chain Bound To Heavy Chain By Disulfide (H-L)
• Heavy Chain Bound to Heavy Chain (H-H)
• First 100 a/a Of Amino Terminal Vary of Both H and L Chain
Are Variable
• Referred To As VL , VH, CH And CL
• CDR (Complementarity Determining Regions) Are What Bind
Ag
• Remaining Regions Are Very Similar Within Same Class
Antibody Structure
• Repeating Domains of ~110 a/a
• Intrachain disulfide bonds within each domain
• Heavy chains
• 1 VH and either 3 or 4 CH (CH1, CH2, CH3, CH4)
• Light chains
• 1 VL and 1 CL
• Hinge Region
• Rich in proline residues (flexible)
• Hinge found in IgG, IgA and IgD
• Proline residues are target for proteolytic digestion (papain and pepsin)
• Rich in cysteine residues (disulfide bonds)
• IgM and IgE lack hinge region
• They instead have extra CH4 Domain
Antibody Structure
Immunoglobulin Functions
• 1. Direct Neutralization - bacterial toxins
- viral particles
• 2. Opsonization - enhancing phagocytosis
• 3. Complement Activation - classical pathway
• 4. Activation Of Cellular Elements
Antibody Classes And Biological Activities
• Immunoglobulins →divided into five different classes → according
to the difference in structure in constant domains of heavy chain
• 1. Gamma heavy chains → IgG
• 2. Alpha heavy chains → IgA
• 3. Mu heavy chains → IgM
• 4. Epsilon heavy chains → IgE
• 5. Delta heavy chains → IgD
• Different classes and subclasses of antibodies perform different
effector functions. There are two types of light chains, called κ (kappa)
and λ (lambda). An antibody has either two κ light chains or two λ light
chains.
Immunoglobulin G
• Most abundant & has the broadest role four
subclasses,
a. IgG & IgG - activate complement
b. IgG & IgG - interact with Ig receptors on
phagocytes
• crosses the placenta,
a. Provides immunity for the neonate
b. Produces rhesus incompatibility disease
Immunoglobulin A
• Predominant Ig found in secretions,
a. Respiratory Tract b. GIT
c. Urinary Tract d. Tears
e. Saliva f. Colostrum
• Exists as a monomer in serum, but as the dimer "secretory-IgA" in
secretions
• 2 units are joined by a J-chain (MW ~ 15,000) then excreted from
plasma cells in the submucosa
• taken-up by epithelial cells and the secretory piece is added
• this effectively makes the molecule resistant to enzymatic degradation
Immunoglobulin M
• A pentamer comprising ~ 10% of circulating Ig
• capable or forming a spontaneous pentamer configuration,
but usually with J-chain
• also exists as a monomeric form in mature B-cells
• Predominantly intravascular & involved in the early immune
response
• Major class of antibodies involved in,
a. Blood Groups - A & B
b. Autoimmune Disease:
- rheumatic fever
- rheumatoid arthritis, etc.
c. Cold Agglutinins
Immunoglobulin D
• predominantly intravascular
• associated with the surface of resting B-cells,
with IgM
• may be important in B-cell Ag binding and
subsequent differentiation to plasma cells
Immunoglobulin E
• Play major role in hypersensitivity
• reactions bind to mast cells via the Fc fragment
• Ag must bind & cross-link 2 antibodies to initiate
mast cell degranulation
Immunoglobulin Subclasses
ANTIGEN-ANTIBODY
REACTIONS
Dr. Taha Abdul-Aziz saeid kaid
Assistant professor of
Microbiology and Medical Immunology

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