6/5/23, 10:44 PM Antibody- Structure, Classes and Functions

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Antibody- Structure, Classes and Functions

Last updated: August 10, 2022 by Sagar Aryal

Antibody (Ab) also know as Immunoglobulin (Ig) is the large Y shaped protein produced by
the body’s immune system when it detects harmful substances, called antigens like bacteria
and viruses. The production of antibodies is a major function of the immune system and is
carried out by a type of white blood cell called a B cell (B lymphocyte), differentiated B cells
called plasma cells. The produced antibodies bind to specific antigens express in external
factors and cancer cells.

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Source: Kyowa Hakko Kirin Co., Ltd

Structure of Antibody
Antibodies are heavy (~150 kDa) globular plasma proteins. The basic structure of all
antibodies are same.

Structure of Antibody.
Source: Kyowa Hakko Kirin Co., Ltd

There are four polypeptide chains: two identical heavy chains and two identical light
chains connected by disulfide bonds. Light Chain (L) consists polypeptides of about 22,000
Da and Heavy Chain (H) consists larger polypeptides of around 50,000 Da or more. There
are five types of Ig heavy chain (in mammal) denoted by the Greek letters: α, δ, ε, γ, and
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μ. There are two types of Ig light chain (in mammal), which are called lambda (λ) and kappa
(κ).

An antibody is made up of a variable region and a constant region, and the region that
changes to various structures depending on differences in antigens is called the variable
region, and the region that has a constant structure is called the constant region.

Structure of Antibody
Source: Sino Biological Inc.

Each heavy and light chain in an immunoglobulin molecule contains an amino-terminal

variable (V) region that consists of 100 to 110 amino acids and differ from one antibody to
another. The remainder of each chain in the molecule – the constant (C) region exhibits
limited variation that defines the two light chain subtypes and the five heavy chains
subclasses. Some heavy chains (α, δ, γ) also contain a proline-rich hinge region. The amino
terminal portions, corresponding to the V regions, bind to antigen; effector functions are
mediated by the carboxy-terminal domains. The ε and μ heavy chains, which lack a hinge
region, contain an additional domain in the middle of the molecule. CHO denotes a
carbohydrate group linked to the heavy chain.

Classes/Types of Antibody
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Serum containing antigen-specific antibodies is called antiserum. The 5 types – IgG, IgM,
IgA, IgD, IgE – (isotypes) are classified according to the type of heavy chain constant region,
and are distributed and function differently in the body.

Functions of Antibody
1. IgG provides long term protection because it persists for months and years after the
prescence of the antigen that has triggered their production.
2. IgG protect against bacteris, viruses, neutralise bacterial toxins, trigger compliment
protein systems and bind antigens to enhance the effectiveness of phagocytosis.
3. Main function of IgA is to bind antigens on microbes before they invade tissues. It
aggregates the antigens and keeps them in the secretions so when the secretion is
expelled, so is the antigen.

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4. IgA are also first defense for mucosal surfaces such as the intestines, nose, and lungs.
5. IgM is involved in the ABO blood group antigens on the surface of RBCs.
6. IgM enhance ingestions of cells by phagocytosis.
7. IgE bind to mast cells and basophils wich participate in the immune response.
8. Some scientists think that IgE’s purpose is to stop parasites.
9. IgD is present on the surface of B cells and plays a role in the induction of antibody
production.

Similar Posts:
Immunoglobulin A (IgA) – Structure, Properties, Subclasses, Functions
Immunoglobulin E (IgE) – Properties, Structure and Functions
Antigen- Properties, Types and Determinants of Antigenicity
Blood cells and its types with functions

 Immunology

12 thoughts on “Antibody- Structure, Classes and Functions”

kat
January 3, 2023 at 11:42 AM

Great article for an overview of antibodies! Thanks for writing this.

Reply

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MIA
June 27, 2019 at 8:04 AM

If IgG is low in its strength ” so to speak” does that mean the virus and or bacterial
infection has surpassed it in the fight to protect the individual….

Reply

Ike Nmesoma Makuo

June 23, 2019 at 11:46 AM

Does all the antibody classes have the same number of constant regions. If no,
please explain to me why with vivid structure of the different antibody classes. It’s
an assignment that I need to submit. Please

Reply

Ego...
May 15, 2019 at 12:05 PM

What does ig stand for…in full

Reply

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Reezy Feezy
July 23, 2019 at 1:10 AM

immunoglobulin

Reply

Abdul khan
June 10, 2020 at 8:53 AM

immunoglobin which means antibody

Reply

Priyansh agrawal
September 20, 2022 at 4:20 PM

Ig means immunoglobulin
Globulin is a protein

Reply

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alexi
August 13, 2018 at 8:36 PM

why does the heavy chain segment show 4 cdr regions when there is only 3?

Reply

Princess
March 12, 2017 at 8:40 PM

why there’s no IgB, IgC, IgF, IgH, IgI, IgJ, IgK, IgL

Reply

58600
January 2, 2019 at 1:15 AM

There are 5 types of heavy chain constant region; Mu, Gamma, Alpha, Epsilon,
Delta. We take the first letter of each Greek letter to denote IgA, IgG, IgE, IgD and
IgM respectively.

Reply

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gautamsager
August 5, 2016 at 9:10 PM

please write names of anti bodies

Reply

Abdul khan
June 10, 2020 at 8:54 AM

antibody G
antibody A
antibody M
antibody E
antibody D
antibody = immunoglobin

Reply

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