Immunoglobulins, also known as antibodies, are Y-shaped glycoproteins produced by plasma cells that function to identify and neutralize foreign objects like bacteria and viruses. Each arm of the Y contains a paratope that binds to a specific epitope on an antigen. There are five classes of immunoglobulins - IgG, IgM, IgA, IgD, and IgE - which differ in their structure and functions like complement fixation, binding to cells, and roles in allergic reactions and parasitic infections. Multiple myeloma is a plasma cell tumor characterized by overproduction of IgG and IgM antibodies and Bence Jones proteins in the serum and urine.
ANTIGEN, HAPTEN, ALL TYPES OF ANTIGENS, IMMUNOGEN , ATTRIBUTES OF ANTIGENICITY, DETERMINANTS OF ANTIGENICITY,
IMMUNOLOGY KUBY, MEDICAL MICROBIOLOGY & IMMUNOLOGY OF PANIKER , LIPPINCOTT'S IMMUNOLOGY, OTHER SOURCES.
This topic covers the brief introduction of Ag and Ab in detail. Types and functions of Ig is explained in detail. Paraproteinemias is explained with simple pictures.
by Dr. N.Sivaranjani, MD
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
Humoral immunity is defined as the immunity mediated by antibodies, which are secreted by B lymphocytes.
B lymphocytes secrete the antibodies into the blood and lymph
BP-605T, Pharmaceutical biotechnology, Structure of immunoglobulins, classification of immunoglobulins, explanation of structure of immunoglobulin, digestion with proteolytic enzymes, Fab region, Fc region, role of different immunoglobulin classes, structure of IGM, IGA, IGG, IGE, IGD, Light chain, heavy chain, kappa, lambda, papain enzyme, pepsin enzyme
ANTIGEN, HAPTEN, ALL TYPES OF ANTIGENS, IMMUNOGEN , ATTRIBUTES OF ANTIGENICITY, DETERMINANTS OF ANTIGENICITY,
IMMUNOLOGY KUBY, MEDICAL MICROBIOLOGY & IMMUNOLOGY OF PANIKER , LIPPINCOTT'S IMMUNOLOGY, OTHER SOURCES.
This topic covers the brief introduction of Ag and Ab in detail. Types and functions of Ig is explained in detail. Paraproteinemias is explained with simple pictures.
by Dr. N.Sivaranjani, MD
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
Humoral immunity is defined as the immunity mediated by antibodies, which are secreted by B lymphocytes.
B lymphocytes secrete the antibodies into the blood and lymph
BP-605T, Pharmaceutical biotechnology, Structure of immunoglobulins, classification of immunoglobulins, explanation of structure of immunoglobulin, digestion with proteolytic enzymes, Fab region, Fc region, role of different immunoglobulin classes, structure of IGM, IGA, IGG, IGE, IGD, Light chain, heavy chain, kappa, lambda, papain enzyme, pepsin enzyme
One of the important parts in the study of Immunology.I prepared it for the sake of a seminar series competition conducted in my university. Now I thought of sharing it with others.
A path breaking technology which has made it possible for us to detect HIV. ELISA is an immunological assay nowadays even used to detect food proteins & is the science behind pregnancy color test. This presentation unlocks the working of this assay.
ELISA Vs ELISPOT - Principle, Procedure, Advantagesajithnandanam
The Enzyme Linked Immunospot (ELISPOT) technique was developed by Cecil Czerkinskdy in 1983. ELISPOT is used for the detection of secreted proteins, such as cytokines and growth factors. ELISPOT is primarily used in immunology research in the following areas:
This presentation clearly describes what are immunoglobulins, their types, structure and how they get diversified into different isotopes to fight with foreign antigens.
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
What is an Antibody?Immunoglobulins: Classes and Sub classesvarinder kumar
Forms
History
Immunoglobulins: Classes and Sub classes
Epitope
Antibodies structure
Antibody–antigen interactions
Function
Medical Applications
Regulations
Preclinical studies
Structure prediction
Antibody mimetic
Another name of anti-body is immunoglobulins . Anti-body is the glycoprotein which is produce by Bcell and which are responsible to bind antigen with higher specifity and affinity. Anti-body is mainly
distrusted in body fluid and also present surface of some cell.
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody.
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody
Antibody (Ab) also known 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.
OUTCOMES
By the end of this session student should be able to know
The structure of antibody
Immunoglobulin classes
Monoclonal antibodies VS polyclonal
INTRODUCTION
Antibodies are globulin proteins (immunoglobulins [Ig]) that react specifically with the antigen that stimulated their production.
They make up about 20% of the protein in blood plasma. Blood contains three types of globulins,
alpha,
beta,
gamma,
Antibodies are gamma globulins.
INTRODUCTION
There are five classes of antibodies:
1. IgG,
2. IgM,
3. IgA,
4. IgD,
5. IgE
Antibodies are subdivided into these five classes based on differences in their heavy chains.
ROLE OF ANTIBODIES
The most important functions of antibodies are to
neutralize toxins and viruses,
to opsonize microbes
so they are more easily phagocytosed, to activate complement, and to prevent the attachment of microbes to mucosal surfaces.
In addition to these functions, antibodies have a catalytic (enzymatic) capability
Antibody Type
IgA
IgD
IgE
IgG
IgM
Function
Found in saliva, tears, mucus, breast milk and intestinal fluid, IgA protects against ingested and inhaled pathogens.
This antibody is found on the surface of your B cells. Though its exact function is unclear, experts think that IgD supports B cell maturation and activation.
Found mainly in the skin, lungs and mucus membranes, IgE antibodies cause your mast cells (a type of white blood cell) to release histamine and other chemicals into your bloodstream. IgE antibodies are helpful for fighting off allergic reactions.
This is the most common antibody, making up approximately 70% to 75% of all immunoglobulins in your body. It’s found mainly in blood and tissue fluids. IgG antibodies help protect your body from viral and bacterial infections.
Found in your blood and lymph system, IgM antibodies act as the first line of defense against infections. They also play a large role in immune regulation.
MONOCLONAL VS POLYCLONAL
A. Polyclonal antibodies contain a heterologous mixture of IgGs against the whole antigen
B. monoclonal antibodies are composed of a single IgG against one epitope.
Polyclonal antibodies
Monoclonal antibodies
Refer to a mixture of immunoglobulin molecules that are secreted against a particular antigen.
Refer to a homogenous population of antibodies that are produced by a single clone of plasma B cells.
Produced by different clones of plasma B cells.
Produced by the same clone of plasma B cells.
A heterogeneous antibody population.
A homogenous antibody population.
Interact with different epitopes on the same antigen.
Interact with a particular epitope on the antigen.
STRUCTURE OF ANTIBODY
Immunoglobulins are glycoproteins made up of
1. light (L)
2. heavy (H) polypeptide chains.
The terms light and heavy refer to molecular weight
STRUCTURE OF ANTIBODY
The simplest antibody molecule has a Y shape consist of
Essentials of Automations: Optimizing FME Workflows with ParametersSafe Software
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https://alandix.com/academic/papers/synergy2024-epistemic/
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2. DEFINITION
Immunoglobulins (Ig) - 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 was placed in an
electrical field the antibodies, which were
responsible for immunity, migrated with the
globular proteins .
3. 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.
4. 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. Using this binding mechanism, an
antibody can tag a microbe or an infected cell for
attack by other parts of the immune system, or
can neutralize its target directly (for example, by
blocking a part of a microbe that is essential for
its invasion and survival).
5. Antibodies can occur in two physical forms, a
soluble form that is secreted from the cell, and a
membrane-bound form that is attached to the
surface of a B cell and is referred to as the B cell
receptor (BCR). The BCR is only found on the
surface of B cells and facilitates the activation of
these cells and their subsequent differentiation
into either antibody factories called plasma cells,
or memory B cells that will survive in the body
and remember that same antigen so the B cells
can respond faster upon future exposure.
6. GENERAL FUNCTIONS OF
IMMUNOGLOBULINS
Ag binding - Immunoglobulins bind
specifically to one or a few closely related
antigens. Each immunoglobulin actually
binds to a specific antigenic determinant.
Antigen binding by antibodies is the primary
function of antibodies and can result in
protection of the host.
7. Effector Functions - Often the binding of an
antibody to an antigen has no direct biological
effect. Rather, the significant biological effects
are a consequence of secondary "effector
functions" of antibodies. The immunoglobulins
mediate a variety of these effector functions.
Usually the ability to carry out a particular
effector function requires that the antibody bind
to its antigen. Not every immunoglobulin will
mediate all effector functions.
8. Fixation of complement - lysis of cells, release of
biologically active molecules
Binding to various cell types - phagocytic cells,
lymphocytes, platelets, mast cells, and basophils
have receptors that bind immunoglobulins and
the binding can activate the cells to perform
some function. Some immunoglobulins also bind
to receptors on placental trophoblasts. The
binding results in transfer of the immunoglobulin
across the placenta and the transferred maternal
antibodies provide immunity to the fetus and
newborn.
9. Nomenclature
Immunoglobulins are named based on the
class, or subclass of the heavy chain and type
or subtype of light chain. Unless it is stated
precisely you are to assume that all subclass,
types and subtypes are present. IgG means
that all subclasses and types are present.
10. Heterogeneity
Immunoglobulins considered as a population
of molecules are normally very
heterogeneous because they are composed
of different classes and subclasses each of
which has different types and subtypes of
light chains. In addition, different
immunoglobulin molecules can have different
antigen binding properties.
11. STRUCTURE
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.
Several immunoglobulin domains make up the
two heavy chains and the two light chains of an
antibody.
The variable parts of an antibody are its V
regions, and the constant part is its C region.
12. Immunoglobulin domains
The Ig monomer is a "Y"-shaped molecule
that consists of four polypeptide chains; two
identical heavy chains and two identical light
chains connected by disulfide bonds.Each
chain is composed of structural domains
called immunoglobulin domains. These
domains contain about 70–110 amino acids.
14. Variable (V) and Constant (C)
Regions
- Each H-chain and each L-chain has V-region
and C-region
- V-region lies in terminal portion of molecule
- V-region shows wide variation in amino a.
sequences
- Responsible for the antigen binding.
- C-region lies in carboxyl or terminal portion of
molecule
- C-region shows an unvarying amino acid
sequence
- It is responsible for biologic functions
15. Immunoglobulin classes
The immunoglobulins can be divided into 5
different classes based on differences in the
amino acid sequences in the constant region
of the heavy chains. All immunoglobulins
within a given class will have very similar
heavy chain constant regions. These
differences can be detected by sequence
studies or more commonly by serological
means (i.e. by the use of antibodies directed
to these differences).
16. 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
18. Immunoglobulin Subclasses
The classes of immunoglobulins can de divided
into subclasses based on small differences in
the amino acid sequences in the constant
region of the heavy chains. All
immunoglobulins within a subclass will have
very similar heavy chain constant region
amino acid sequences. Again these
differences are most commonly detected by
serological means.
19. 1. IgG Subclasses
a) IgG1 - Gamma 1 heavy chains
b) IgG2 - Gamma 2 heavy chains
c) IgG3 - Gamma 3 heavy chains
d) IgG4 - Gamma 4 heavy chains
20. 2. IgA Subclasses
a) IgA1 - Alpha 1 heavy chains
b) IgA2 - Alpha 2 heavy chains
21. C. Immunoglobulin Types -
Immunoglobulins can also be classified by the
type of light chain that they have. Light chain
types are based on differences in the amino
acid sequence in the constant region of the
light chain. These differences are detected by
serological means.
1. Kappa light chains
2. Lambda light chains
22. D. Immunoglobulin Subtypes - The light chains
can also be divided into subtypes based on
differences in the amino acid sequences in the
constant region of the light chain.
1. Lambda subtypes
a) Lambda 1
b) Lambda 2
c) Lambda 3
d) Lambda 4
23. STRUCTURE AND SOME PROPERTIES
OF IgG CLASS
Most versatile immunoglobulin because it is
capable of carrying out all of the functions of
immunoglobulin molecules.
a) IgG is the major Ig in serum - 75% of serum
Ig is IgG
b) IgG is the major Ig in extra vascular spaces.
c) Placental transfer - IgG is the only class of
Ig that crosses the placenta. Transfer is
mediated by receptor on placental cells for
the Fc region of IgG.
24. d) Fixes complement - Not all subclasses fix
equally well; IgG4 does not fix complement
e) Binding to cells - Macrophages,
monocytes, PMN's and some lymphocytes
have Fc receptors for the Fc region of IgG.
Not all subclasses bind equally well; IgG2 and
IgG4 do not bind to Fc receptors.
25. IgA
a) IgA is the 2nd most common serum Ig.
b) IgA is the major class of Ig in secretions -
tears, saliva, colostrum, mucus. Since it is
found in secretions secretory IgA is important
in local (mucosal) immunity.
c) Normally IgA does not fix complement,
unless aggregated.
d) IgA can bind to some cells - PMN's and
some lymphocytes.
26. IgD
1. Structure -. IgD exists only as a monomer.
2. Properties
a) IgD is found in low levels in serum; its role in
serum is uncertain.
b) IgD is primarily found on B cell surfaces where
it functions as a receptor for antigen. It has been
shown to activate basophils and mast cells to
produce antimicrobial factors
c) IgD does not bind complement.
27. IgM
a) IgM is the 3rd most common serum Ig.
b) IgM is the first Ig to be made by the fetus.
c) 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.
d) As a consequence of its structure, IgM is also a
good agglutinating Ig . Thus, IgM antibodies are
very good in clumping microorganisms for
eventual elimination from the body.
28. IgE
1. Structure -. IgE exists as a monomer and has an
extra domain in the constant region.
a) IgE is the least common serum Ig since it binds
very tightly to Fc receptors on basophils and mast
cells even before interacting with antigen.
b) Involved in allergic reactions - As a consequence
of its binding to basophils and mast cells, IgE is
involved in allergic reactions. Binding of the allergen
to the IgE on the cells results in the release of various
pharmacological mediators that result in allergic
symptoms.
29. c) IgE also plays a role in parasitic helminth
diseases. Since serum IgE levels rise in
parasitic diseases, measuring IgE levels is
helpful in diagnosing parasitic infections.
d) IgE does not fix complement.
30. MULTIPLE MYELOMA
Plasma cell tumor.
IgG & IgM Overproduction.
BENCE JONES proteins in serum and urine.