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(Dheeraj) Introduction to Antibodies

Antibodies, or immunoglobulins, are crucial components of adaptive immunity produced by B cells to recognize and neutralize antigens. They have a Y-shaped structure with constant and variable regions, and there are five major classes: IgG, IgM, IgA, IgE, and IgD, each with specific functions and characteristics. IgG is the most abundant and plays a key role in long-term immunity, while IgM is the first responder during infections, and IgA protects mucosal surfaces.

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4 views

(Dheeraj) Introduction to Antibodies

Antibodies, or immunoglobulins, are crucial components of adaptive immunity produced by B cells to recognize and neutralize antigens. They have a Y-shaped structure with constant and variable regions, and there are five major classes: IgG, IgM, IgA, IgE, and IgD, each with specific functions and characteristics. IgG is the most abundant and plays a key role in long-term immunity, while IgM is the first responder during infections, and IgA protects mucosal surfaces.

Uploaded by

anuragchaurasiya846
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPTX, PDF, TXT or read online on Scribd
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Introduction to Antibodies

Antibodies, or immunoglobulins (Ig), are vital to adaptive immunity.


They are produced by B cells when facing antigens. Their main role
is recognizing and neutralizing foreign invaders. Discovered in the
1890s, Ehrlich earned a Nobel Prize in 1908 for this breakthrough.

by Dheeraj chaudhry

B.Sc Biotech (6th sem.)


Antibody Structure
• Constant regions (Fc) define antibody class
Antibodies have a Y-shaped structure with four
polypeptide chains: two heavy and two light chains. • Variable regions (Fab) bind specific antigens
Disulfide bonds hold these chains together, creating • Molecular weight ~150 kDa
stable binding sites.
Antibody-Antigen
Interaction
Specific Binding Affinity vs Avidity
Antibodies attach to Affinity is the strength of
antigens at the paratope one bond; avidity reflects
with high specificity. the total binding strength
of multiple sites.

Lock-and-Key Model
Binding follows a precise fit like a lock and key, enabling
targeted immune response.
Five Major Antibody Classes
(Isotypes)
IgG
Most abundant, provides systemic immunity.

IgM
First responder in infections, pentameric structure.

IgA
Protects mucosal surfaces, present in secretions.

IgE & IgD


Specialized roles in allergies and B cell activation.
IgG: The Workhorse Antibody
• Accounts for 70-80% of serum antibodies
IgG plays a crucial role in long-term immunity and
• Crosses placenta for passive newborn immunity vaccine response. Its ability to cross the placenta
• Functions: opsonization, neutralization, complement protects infants during early life.
activation
• Four subclasses: IgG1, IgG2, IgG3, IgG4
• Long half-life (~21 days)
IgM: First Responder and
Potent Activator
Early Infection Structure & Function
Defense
IgM is the first antibody Has 10 antigen-binding
formed during infection, sites; excels in activating
making up 10% of serum complement proteins.
antibodies.

Location & Lifetime


Primarily found in blood, with a half-life around 5 days.
IgA: Mucosal Immunity
Location
Predominantly in mucosal secretions like saliva and tears.

Structure
Dimeric form in secretions enhances pathogen neutralization.

Function
Provides critical mucosal defense and passive infant
immunity.

Subclasses
IgA1 and IgA2 with distinct distribution and roles.
IgE and IgD: Specialized Roles
IgE IgD

• Involved in allergies and parasite defense • Role not fully understood


• Binds mast cells and basophils • Expressed on mature B cell surfaces
• Triggers histamine release • May aid in B cell activation
• Serum half-life ~2 days; longer bound to cells • Serum half-life ~3 days

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