An

antibody (Ab), also known as an immunoglobulin (Ig), is a large Y-shaped protein produced by B-cells that is used by the immune system to identify and neutralize foreign objects such as bacteria and viruses. The antibody recognizes a unique part of the foreign target, called an antigen. Each tip of the "Y" of an antibody contains a paratope (a structure analogous to a lock) that is specific for one particular epitope(similarly analogous to a key) on an antigen, allowing these two structures to bind together with precision.

 The paratope is the part of an antibody which

recognizes an antigen, the antigen-binding site of an antibody. An epitope, also known as antigenic determinant, is the part of an antigen that is recognized by the immune system, specifically by antibodies, B cells, or T cells. Antibodies are heavy (~150 kDa) globular plasma proteins. They have sugar chains added to some of their amino acid residues. In other words, antibodies are glycoproteins. Antibodies are secreted by a type of white blood cell called a plasma cell The production of antibodies is the main function of the humoral immune system

STRUCTURE OF ANTIBODY:
Disulfide bond Carbohydrate

CL

VL CH2
Hinge Region

CH1

CH3

VH

STRUCTURE OF ANTIBODY
1. Fab region

2. Fc region 3. Heavy chain (blue) with one variable (VH) domain followed by a constant domain (CH1), a hinge region, and two more constant (CH2 and CH3) domains. 4. Light chain (green) with one variable (VL) and one constant (CL) domain 5. Antigen binding site (paratope) 6. Hinge regions.

 1. HEAVY AND LIGHT CHAINS : All immunoglobulins have a four chain structure as their

basic unit. They are composed of two identical small light chains (23kD) and two identical large heavy chains (50-70kD)
Heavy Chain: There are five types of mammalian Ig heavy chain denoted by

the Greek letters: , , , , and . The type of heavy chain present defines the class of antibody; these chains are found in IgA, IgD, IgE, IgG, and IgM antibodies, respectively Light Chain: In mammals there are two types of immunoglobulin light chain, which are called lambda () and kappa ().

 2.DISULFIDE BONDS The heavy and light chains and the two heavy chains are

held together by inter-chain disulfide bonds 3.VARIABLE (V) AND CONSTANT (C) REGIONS The heavy and light chain could be divided into two regions based on variability in the amino acid sequences. These are the: 1. Light Chain - VL (110 amino acids) and CL (110 amino acids) 2. Heavy Chain - VH (110 amino acids) and CH (330-440 amino acids) Most H chains consist of one variable (VH) and three constant(CH) domains.(IgG and IgA have three CH domains,whereas IgM and IgE have four.)

 The

variable regions are responsible for antigenbinding ,whereas the constant regions are responsible for various biologic functions eg, complement activation and binding to cell surface receptors.

4.Fab Region: The arms of the Y contain the sites that can bind two

antigens (in general, identical) and, therefore, recognize specific foreign objects. This region of the antibody is called the Fab (fragment, antigen binding) region. It is composed of one constant and one variable domain from each heavy and light chain of the antibody

 5.Fv Region:
The paratope is shaped at the amino terminal end of

the antibody monomer by the variable domains from the heavy and light chains. The variable domain is also referred to as the FV region and is the most important region for binding to antigens. 6. Fc Region: The base of the Y plays a role in modulating immune cell activity. This region is called the Fc (Fragment, crystallizable) region. the Fc region ensures that each antibody generates an appropriate immune response for a given antigen, by binding to a specific class of Fc receptors.

CLASSES OF IMMUNOGLOBINS:
The immunoglobulins can be divided into five

different classes, based on differences in the amino acid sequences in the constant region of the heavy chains. 1. IgG Gamma() heavy chains 2. IgM Mu() heavy chains 3. IgA Alpha() heavy chains 4. IgD Delta() heavy chains 5. IgE Epsilon() heavy chains

IgG
Structure: Monomer (7s)

IgG1, IgG2 and IgG4

IgG3

Properties:
IgG Is the Major Antibody in the Blood, but It Is Able

to Enter Tissue Spaces and Coat Antigens, Speeding Antigen Uptake Molecular weight: 150,000 H-chain type (MW): gamma (53,000) In its four forms, provides the majority of antibody-based immunity against invading pathogens. The only antibody capable of crossing the placenta to give passive immunity to the fetus Fixes complement - Not all subclasses fix equally well; IgG4 does not fix complement

 Representing approximately 75% of serum immunoglobulins in humans, IgG is the

most abundant antibody isotype found in the circulation.

IgG consists of four subclasses (isotypes),

which are numbered in order of their serum concentrations (IgG1, IgG2, IgG3, and IgG4)

IgG molecules are synthesized and secreted by plasma B cells. Binds to Fc receptors on phagocytic cells.

IgG is the predominant immunoglobulin in blood, lymph, peritoneal fluid, and cerebrospinal fluid.

IgM:

Structure Pentamer (19S) composed of 5 H2L2 units plus one molecule of J chain Extra domain (CH4) J chain-This chain functions in polymerization of the molecule into a pentamer.

Properties of IgM:
3rd highest serum Ig IgM is the first antibody to appear during an immune

response and the first formed by a developing fetus. IgM acts as one of the main receptors on the surface of mature B cells, along with IgD. When IgM is a surface receptor, it is in its monomeric form. First Ig made by fetus and B cells IgM is the most versatile antibody and almost certainly the first type of immunoglobulin to have developed evolutionarily. As a consequence of its pentameric structure, IgM is a good complement fixing Ig. Thus, IgM antibodies are very efficient in leading to the lysis of microorganisms.

 Produced early in the primary response The most efficient Ig. because of the J chain, it is also important as a

secretory immunoglobulin Since secretory immunoglobulins are present in breast milk as well, IgM also participates significantly in protecting the newborn from intestinal pathogens

IgA:
Serum - monomer Secretions (sIgA) Dimer (11S), sIgA molecule consists of two H2L2

units plus one molecule each of J chain and secretory component(SC or SP)

Secretory Piece

J Chain

Properties of IgA
2nd highest serum Ig the IgA which is made in the plasma cell, the secretory piece is made in epithelial cells and is added to the IgA as it passes into the secretions . The secretory piece helps IgA to be transported across mucosa and also protects it from degradation in the secretions. Major secretory Ig ( saliva, tears, respiratory, intestinal, and genital tract secretions.) Does not fix complement unless aggregated Binds to Fc receptors on some cells

IgD:
Structure Monomer Tail piece

Tail Piece

Properties 4th highest serum Ig B cell surface Ig Does not bind complement

IgE:
Structure Monomer Extra domain (CH4)

Properties Least common serum Ig Allergic reactions Parasitic infections Does not fix complement

CH4

Summary of functions:
IgG: In its four forms, provides the majority of antibody-based

immunity against invading pathogens. The only antibody capable of crossing the placenta to give passive immunity to fetus. IgM: Expressed on the surface of B cells (monomer) and in a secreted form (pentamer) with very high avidity. Eliminates pathogens in the early stages of B cell mediated (humoral) immunity before there is sufficient IgG IgA: Found in mucosal areas, such as the gut, respiratory tract and urogenital tract, and prevents colonization by pathogens.Also found in saliva, tears, and breast milk. IgD: Functions mainly as an antigen receptor on B cells that have not been exposed to antigens.It has been shown to activate basophils and mast cells to produce antimicrobial factors. IgE: Binds to allergens and triggers histamine release from mast cells and basophils, and is involved in allergy. Also protects against parasitic worms.