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1 General characteristic of immune

system; cellular and humoral
factor
The immune system is a complex network of cells, tissues, and organs that work
together to defend the body against infections, diseases, and other foreign substances.
Some general characteristics of the immune system include:

1. Specificity: The immune system is able to recognize and respond to specific

antigens, which are substances that trigger an immune response.

2. Diversity: The immune system is able to recognize a vast array of antigens, which
allows it to respond to a wide range of pathogens.

3. Memory: The immune system is able to "remember" antigens it has encountered

before and mount a faster and more effective response upon subsequent exposure.

4. Self-tolerance: The immune system is able to distinguish between self and non-self
antigens and avoid attacking the body's own cells and tissues.

5. Complex regulation: The immune system is regulated by a complex network of cells

and molecules that work together to ensure a balanced and appropriate response.

6. Rapid response: The immune system is able to mount a rapid response to

pathogens and other threats, which is important for preventing the spread of
infections.

Humoral immunity
As the antigens bind to B-lymphocytes, they
trigger the production of antibodies which
can destroy the pathogens. Some of the
B-lymphocytes become memory cells that can
protect the host against future infections.
Cellular immunity
The protein fragments of the antigen bound to
MHC molecules can activate the cytotoxic
T-lymphocytes. They are capable of destroying

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 the infected pathogenic cells. Some of
the activated T-lymphocytes become memory
cells which can kill the future infecting
pathogens

2.Immunoglobulins: structure,
biological function, mechanisms of
immunoglobulin synthesis.
Characteristics of distinct
immunoglobulin classes of human
blood.
Immunoglobulins—basic concepts
Immunoglobulins, a specialised group of
proteins are mostly associated with J-globulin
fraction (on electrophoresis) of plasma proteins.
Some immunoglobulins however, separate along
with E and D-globulins. Therefore, it should be
noted that J-globulin and immunoglobulin
are not synonymous. Immunoglobulin is a
functional term while J-globulin is a physical
term.
Structure of immunoglobulins
All the immunoglobulin (Ig) molecules
basically consist of two identical heavy (H)
chains (mol. wt. 53,000 to 75,000 each) and two
identical light (L) chains (mol. wt. 23,000 each)
held together by disulfide linkages and noncovalent interactions (Fig.9.3). Thus,
immunoglobulin is a Y-shaped tetramer (H2L2). Each
heavy chain contains approximately 450 amino
acids while each light chain has 212 amino
acids. The heavy chains of Ig are linked to
carbohydrates, hence immunoglobulins are
glycoproteins

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 Constant and variable regions : Each chain
(L or H) of Ig has two regions (domains), namely
the constant and the variable. The amino
terminal half of the light chain is the variable
region (VL) while the carboxy terminal half is the
constant region (CL). As regards heavy chain,
approximately one-quarter of the amino terminal region is variable (VH) while the
remaining threequarters is constant (CH1, CH2, CH3). The amino acid sequence (with
its tertiary structure) of variable regions of light and heavy chains is responsible for the
specific binding of
immunoglobulin (antibody) with antigen.

proteolytic cleavage of Ig : An immunoglobulin can be split by the enzyme papain to

their fragments. These are two identical antigen
binding fragments (Fab) and one crystallizable
fragment (Fc). Papain cleaves the immunoglobin
molecule at the site between CH1 and CH2
regions which is referred to as hinge region

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 Characteristics of distinct
immunoglobulin classes of human
blood.

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 Immunoglobulin G (IgG)
IgG is the most abundant (75–80%) class of
immunoglobulins. IgG is composed of a single
Y-shaped unit (monomer). It can traverse blood
vessels readily. IgG is the only immunoglobulin
that can cross the placenta and transfer the
mother’s immunity to the developing fetus. IgG
triggers foreign cell destruction mediated by
complement system.

Immunoglobulin A (IgA)
IgA occurs as a single (monomer) or double
unit (dimer) held together by J chain. It is mostly
found in the body secretions such as saliva, tears, sweat, milk and the walls of
intestine. IgA is the most predominant antibody in the colostrum, the initial secretion
from the mother’s breast after a baby is born. The IgA molecules bind with
bacterial antigens present on the body (outer
epithelial) surfaces and remove them. In this
way, IgA prevents the foreign substances from
entering the body cells.
Immunoglobulin M (IgM)
IgM is the largest immunoglobulin composed
of 5 Y-shaped units (IgG type) held together by
a J polypeptide chain. Thus IgM is a pentamer.
Due to its large size, IgM cannot traverse blood
vessels, hence it is restricted to the blood stream

IgM is the first antibody to be produced in

response to an antigen and is the most effective
against invading microorganisms. It may be
noted that IgM can simultaneously combine with
5 antigenic sites due to its pentameric structure.

Immunoglobulin D (IgD)
IgD is composed of a single Y-shaped unit
and is present in a low concentration in the
circulation. IgD molecules are present on the

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 surface of B cells. Their function, however, is not
known for certain. Some workers believe that
IgD may function as B-cell receptor

Immunoglobulin E (IgE)
IgE is a single Y-shaped monomer. It is normally
present in minute concentration in blood. IgE levels
are elevated in individuals with allergies as it is
associated with the body’s allergic responses. The
IgE molecules tightly bind with mast cells which
release histamine and cause allergy

biological function
Immunoglobulins, also known as antibodies, are proteins produced by B lymphocytes (B
cells) in response to the presence of specific antigens. The biological function of
immunoglobulins is to recognize and bind to these antigens, marking them for
destruction by other components of the immune system. Some of the key functions of
immunoglobulins include:

1. Neutralization: Immunoglobulins can neutralize the activity of toxins and viruses by

binding to their surface and preventing them from interacting with host cells.

2. Opsonization: Immunoglobulins can coat pathogens and other foreign substances,

making them more recognizable to phagocytes such as macrophages and
neutrophils, which then engulf and destroy the coated particles.

3. Complement activation: Immunoglobulins can activate the complement system,

which is a group of proteins that work together to destroy pathogens through a
series of biochemical reactions.

4. Allergy and inflammation: In some cases, immunoglobulins can contribute to allergic

reactions and inflammation by binding to allergens and triggering the release of
histamine and other pro-inflammatory molecules.

Overall, the biological function of immunoglobulins is to recognize and respond to a

wide range of antigens, and to coordinate and enhance the activity of other components
of the immune system in order to eliminate these foreign substances and protect the
body from infection and disease.

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 mechanisms of
immunoglobulin synthesis.
Immunoglobulins, also known as antibodies, are proteins produced by B lymphocytes (B
cells) in response to the presence of specific antigens. The synthesis of
immunoglobulins involves several mechanisms, including:

1. B cell activation: When a B cell encounters an antigen, it becomes activated and

begins to divide and differentiate into plasma cells, which are specialized cells that
produce and secrete immunoglobulins.

2. Gene rearrangement: Each B cell has multiple genes that encode for different
regions of the immunoglobulin molecule, including the variable (V), diversity (D),
joining (J), and constant (C) regions. During B cell development, these genes
undergo rearrangement to create a unique combination of V, D, and J regions,
which determines the specificity of the immunoglobulin for a particular antigen.

3. Transcription and translation: Once the B cell has undergone gene rearrangement,
it begins to transcribe and translate the genes into the primary immunoglobulin
transcript. This transcript is then processed and modified to create the mature
immunoglobulin protein.

4. Assembly and secretion: The immunoglobulin protein is assembled and packaged

into vesicles, which are then transported to the cell surface and secreted into the
extracellular space. Once released, the immunoglobulin can bind to its specific
antigen and initiate an immune response.

Overall, the synthesis of immunoglobulins is a complex process that involves several

mechanisms of gene regulation, transcription, translation, and protein processing.

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 3. Mediators and hormones of
immune system (interleukins,
interferons, protein and peptide
factors of cell growth and
proliferation).
The immune system relies on a complex network of mediators and hormones to
coordinate immune responses, including:

1. Interleukins: Interleukins are a group of signaling proteins that are produced by

various cells of the immune system, including T cells, B cells, and macrophages.
They play a key role in regulating immune responses, including inflammation, cell
proliferation, and differentiation.

2. Interferons: Interferons are a group of signaling proteins that are produced by cells
in response to viral infections and other pathogens. They have antiviral and
immunomodulatory effects, and can enhance the activity of immune cells such as
natural killer cells and T cells.

3. Tumor necrosis factor (TNF): TNF is a cytokine that is produced by macrophages

and other cells in response to infection, inflammation, and other types of cellular

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 stress. It has a variety of effects on immune cells, including stimulating inflammation
and promoting cell death.

4. Growth factors: Growth factors are a group of proteins that are involved in cell
growth, differentiation, and proliferation. They include factors such as epidermal
growth factor (EGF), platelet-derived growth factor (PDGF), and transforming
growth factor-beta (TGF-beta), among others. These factors play a key role in
regulating the growth and differentiation of immune cells, as well as in tissue repair
and regeneration.

Overall, the mediators and hormones of the immune system play critical roles in
coordinating and regulating immune responses, and disruptions in these signaling
pathways can lead to a range of immune disorders and diseases.

4. Factors of complement system.

Classical and alternative pathways
of complement activation
THE COMPLEMENT SYSTEM
The complement system is composed of about
20 plasma proteins that ‘complement’ the
function of antibodies in defending the body
from the invading antigens. The complementary
factors are heat labile and get inactivated if
heated at 56°C for about 30 minutes. The
complement system helps the body immunity in
4 ways

1. Complement fixation : The complement

system binds to the foreign invading cells and
causes lysis of the cell membranes.

2. Opsonization : The process of promoting

the phagocytosis of foreign cells is referred to as
opsonization.

3. Inflammatory reaction : The complement

system stimulates local inflammatory reaction
and attracts phagocytic cells.

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 4. Clearance of antigen-antibody complexes :
The complement system promotes the clearance
of antigen-antibody complexes from the body.
Nomenclature of complement system : The
complement proteins are designated by the letter
‘C’, followed by a component number—C1, C2,
C3 etc.
Types of reaction : The complement system
brings about two sets of reactions :

5. Antibody dependent classical pathway.

6. Antibody independent alternative pathway.

Each one of the pathways consists of a series
of reactions converting inactive precursors to
active products by serine proteases which
resembles blood coagulation

Classical and alternative pathways

of complement activation.

The complement system is a key part of the immune system that helps to identify and
eliminate pathogens. There are three pathways of complement activation: the classical
pathway, the lectin pathway, and the alternative pathway.

1. Classical pathway: The classical pathway is activated when antibodies, such as IgG
or IgM, bind to a pathogen surface. The antibodies then recruit and activate the
complement protein C1, which triggers a cascade of complement activation that
ultimately leads to the formation of the membrane attack complex (MAC). The MAC
can directly damage and kill the pathogen.

2. Alternative pathway: The alternative pathway is activated by the presence of certain

molecules on the surface of pathogens, such as bacterial endotoxins or viral
particles. These molecules trigger the activation of the complement protein C3,
which begins a cascade of complement activation that ultimately leads to the
formation of the MAC. The alternative pathway can also be activated by the
spontaneous hydrolysis of C3 in the absence of a pathogen.

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 Both the classical and alternative pathways converge on the formation of the C3
convertase, which cleaves C3 into C3a and C3b fragments. C3b then binds to the
surface of the pathogen, leading to the assembly of the MAC and direct damage to the
pathogen.

1. Lectin pathway: The lectin pathway is similar to the classical pathway in that it
requires the binding of a pattern recognition molecule to a pathogen surface. The
pattern recognition molecule in this pathway is mannose-binding lectin (MBL), which
binds to specific carbohydrates on the surface of pathogens. MBL then recruits and
activates the complement protein C2, which triggers a cascade of complement
activation that ultimately leads to the formation of the MAC.

All three pathways of complement activation ultimately lead to the same endpoint: the
formation of the MAC, which can directly destroy pathogens. However, the pathways
differ in their triggers and in the complement proteins involved in their activation.

5 Biochemical mechanisms of
immunodeficiencies: primary
(hereditary) and secondary
immunodeficiencies; acquired
immunodeficiency syndrome (AIDS).
The immune system is responsible for protecting the body against infections and other
threats. However, in some cases, the immune system can fail to function properly,
resulting in immunodeficiency disorders. There are two main types of
immunodeficiencies: primary (hereditary) and secondary immunodeficiencies.

1. Primary (hereditary) immunodeficiencies: Primary immunodeficiencies are genetic

disorders that affect the development or function of the immune system. These
disorders are usually present from birth and are caused by mutations in genes that
are involved in immune system function. Examples of primary immunodeficiencies
include severe combined immunodeficiency (SCID), common variable
immunodeficiency (CVID), and X-linked agammaglobulinemia.

2. Secondary immunodeficiencies: Secondary immunodeficiencies are acquired

disorders that result from external factors such as infections, medications, or other

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 medical conditions. These disorders can affect the functioning of the immune
system by either impairing its ability to fight infections or causing it to attack the
body's own tissues. Examples of secondary immunodeficiencies include HIV/AIDS,
certain cancers, and autoimmune disorders.

While primary immunodeficiencies are usually genetic and present from birth,
secondary immunodeficiencies can occur at any time during a person's life and can be
caused by a wide range of factors. Both types of immunodeficiencies can lead to
increased susceptibility to infections and other health problems, and may require
medical treatment and management
acquired
immunodeficiency syndrome (AIDS).

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 6 The role of immune system in
pathogenesis of COVID-19

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29b-be64-f8efe2712122/1-s2.0-S0024320520306500-main.pdf

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