Immunoglobulins are glycoprotein molecules produced by plasma cells that function as antibodies. They have a basic Y-shaped structure composed of two heavy chains and two light chains connected by disulfide bonds. The variable regions at the tips of the Y determine antigen binding specificity. The constant regions define the five major classes - IgG, IgM, IgA, IgD, and IgE - which have different effector functions like complement activation. IgG is the most abundant antibody and provides systemic immunity while IgA dominates mucosal immunity. IgE mediates allergic reactions by binding to mast cells and basophils.
An antibody (Ab), also known as an immunoglobulin (Ig), is a Y-shaped protein produced mainly by B- plasma cells that is used to neutralize pathogens such as bacteria, viruses etc.These slides will reflect the introduction, structure and types of antibodies.
An antibody (Ab), also known as an immunoglobulin (Ig), is a Y-shaped protein produced mainly by B- plasma cells that is used to neutralize pathogens such as bacteria, viruses etc.These slides will reflect the introduction, structure and types of antibodies.
immunoglobulin are produce by the body against specific stimuli i.e antigen. antibody are of different types and these are classify according to there nature, temperature of reaction, structure and crossing of placenta. antibody are of Y shaped structure which is composed of different region. classification is based on the type of heavy chain, there are 5 major classes of antibodies, IgA, Igd, Igm, ige, most important of these are igm and igg, although each and every have there own significance.
G Proteins - Dr. P. Saranraj, Assistant Professor, Department of Microbiology, Sacred Heart College (Autonomous), Tirupattur, Vellore District, Tamil Nadu, India.
immunoglobulin are produce by the body against specific stimuli i.e antigen. antibody are of different types and these are classify according to there nature, temperature of reaction, structure and crossing of placenta. antibody are of Y shaped structure which is composed of different region. classification is based on the type of heavy chain, there are 5 major classes of antibodies, IgA, Igd, Igm, ige, most important of these are igm and igg, although each and every have there own significance.
G Proteins - Dr. P. Saranraj, Assistant Professor, Department of Microbiology, Sacred Heart College (Autonomous), Tirupattur, Vellore District, Tamil Nadu, India.
Immunology is the study of the immune system and is a very important branch of the medical and biological sciences. The immune system protects us from infection through
Immunology is the study of the immune system and is a very important branch of the medical and biological sciences. The immune system protects us from infection through
Immunology is the study of the immune system and is a very important branch of the medical and biological sciences. The immune system protects us from infection through
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3. Immunoglobulins:Structure and Function
• Definition: Glycoprotein molecules that are
produced by plasma cells in response to an
immunogen and which function as antibodies
Immune serum
Ag adsorbed serum
α1 α2 β γ
+ -
albumin
globulins
Mobility
Amountofprotein
4. General Functions of
Immunoglobulins
• Ag binding
– Can result in protection
– Valence-binding sites on Ag for Ab/ on Ab for
Ag
• Effector functions (Usually require Agbinding)
– Fixation of complement
– Binding to various cells
6. Immunoglobulin Structure
• Heavy & Light
Chains
• Disulfide bonds
– Inter-chain
– Intra-chain
CH1
VL
CL
VH
CH2 CH3
Hinge Region
Carbohydrate
Disulfide bond
7. Immunoglobulin Structure
• Variable &
Constant Regions
– V & CL L
– VH& CH
• Hinge Region
CH1
VL
CL
VH
CH2 CH3
Hinge Region
Carbohydrate
Disulfide bond
8. Immunoglobulin Structure
• Domains
– VL& CL
– VH& CH1- CH3
(or CH4)
• Oligosaccharides CH1
VL
CL
VH
CH2 CH3
Hinge Region
Carbohydrate
Disulfide bond
9. IgG molecule
Used with permission from: Dr. Mike Clark, Immunology
Division, Department of Pathology Cambridge University,
Cambridge, England
10. Structure of the Variable Region
• Hypervariable (HVR) or complimentarity
determining regions (CDR) HVR3
FR1 FR2 FR3 FR4
HVR2
VariabilityIndex
25 75 10050
Amino acid residue
150
100
HVR1
50
0
• Framework regions
14. Human Immunoglobulin Classes
• IgG - Gamma (γ) heavy chains
• IgM - Mu (µ) heavy chains
• IgA - Alpha (α) heavy chains
• IgD - Delta (δ) heavy chains
• IgE - Epsilon (ε) heavy chains
15. Human Immunoglobulin Subclasses
• IgG Subclasses
– IgG1 - Gamma 1 (γ1) heavy chains
– IgG2 - Gamma 2 (γ2) heavy chains
– IgG3 - Gamma 3 (γ3) heavy chains
– IgG4 - Gamma 4 (γ4) heavy chains
• IgA subclasses
– IgA1 - Alpha 1 (α1) heavy chains
– IgA2 - Alpha 2 (α2) heavy chains
22. IgM
• Structure
• Properties
– 3rd highest serum Ig
– First Ig made by fetus and B cells in
acute infection
– Fixes complement
23. Fixation of C1 by IgG and IgM Abs
C1q
C1q
No activation Activation
24. IgM
Tail
Piece
• Structure
• Properties
– 3rd highest serum Ig
– First Ig made by fetus
and B cells
– Fixes complement
– Agglutinating Ig
– Binds to Fc receptors
– B cell surface Ig
28. IgA
• Structure
• Properties
– 2nd highest serum Ig
– Major secretory Ig (Mucosal or Local Immunity)
• Tears, saliva, gastric and pulmonary secretions
– Does not fix complement (unless aggregated)
– Binds to Fc receptors on some cells
32. IgE
• Structure
• Properties
– Least common serum Ig
• Binds to basophils and mast cells (Does not require
Ag binding)
– Allergic reactions
– Parasitic infections (Helminths)
• Binds to Fc receptor on eosinophils
– Does not fix complement