dr Budi Enoch SpPD

Immunology
dr Budi Enoch SpPD

the defence mechanisms

• Immunology is the branch of biomedical science that
deals with the response of an organism to antigenic
challenge and its recognition of what is self and what
is not.
• It deals with the defence mechanisms including all
physical, chemical and biological properties of the
organism that help it to combat its susceptibility to
foreign organisms, material, etc.
• The word immunity was derived from the Lain word
“immunis” meaning exempt (dibebaskan).
• Title: MRSA, Ingestion by Neutrophil Description: MRSA (yellow) being
ingested by neutrophil (purple).
• Photo Source: National Institute of Allergy and Infectious Diseases (NIAID)
 Innate and adaptive immune systems
• The immune system is divided into those which are static,
or innate to the organism, and those which are responsive,
or adaptive to a potential pathogen or foreign substance.
1. The innate system of immunity is on evolutionary terms, the
older system that forms the first line of defence.
It is non-specific and the resistance is static (it does not improve with
repeated exposure and there is no memory on subsequent exposures).
This includes physical defences such as skin & epithelial surfaces, cilia,
commensual flora, acidic gastric contents, fever etc. Others are
biochemical defences such as soluble - lysosyme, acute phase reactants
and complement, fibronectin, interferons. Cellular components include
natural killer cells, RES phagocytes.
2. The adaptive system is the second line of defence and is
activated once the innate system has been overwhelmed. It is
specific to the infective agent and can store the information
about the invader as memory to show an enhanced response to
subsequent challenge.
The innate system
Key lymphoid organs of the immune system

• The key primary lymphoid organs of the immune system

are thymus and bone marrow, and secondary lymphatic
tissues such as spleen, tonsils, lymph vessels, lymph
nodes, adenoids, and skin.
• In good health thymus, spleen, portions of bone marrow,
lymph nodes and secondary lymphatic tissues can be
surgically removed without much harm to humans.
• The actual components of the immune system are cellular
in nature and not associated with any specific organ. They
are widely present in circulation throughout the body.
 Classical immunology
• Classical immunology ties in with the fields
of epidemiology and medicine. It studies the relationship between the
body systems,pathogens, and immunity. The earliest written mention of
immunity can be traced back to the plague of Athens in 430 BCE.
• Thucydides noted that people who had recovered from a previous bout
of the disease could nurse the sick without contracting the illness a
second time.
• Many other ancient societies have references to this phenomenon, but it
was not until the 19th and 20th centuries before the concept developed
into scientific theory.
• The study of the molecular and cellular components that comprise the
immune system, including their function and interaction, is the central
science of immunology. The immune system has been divided into a more
primitive innate immune system and, invertebrates, an acquire or
adaptive immune system.
• The latter is further divided into humoral (or antibody) and cell-mediated
components.
• The humoral (antibody) response is defined as the interaction
between antibodies and antigens.
• Antibodies are specific proteins released from a certain class of
immune cells known as B lymphocytes, while antigens are
defined as anything that elicits the generation of antibodies
("anti"body "gen"erators).
• Immunology rests on an understanding of the properties of these
two biological entities and the cellular response to both.
• Immunological research continues to become more specialized,
pursuing non-classical models of immunity and functions of cells,
organs and systems not previously associated with the immune
system (Yemeserach 2010).
• Humoral immune response due to activation of B cells leads to
production of humoral or antibody-mediated immunity, and cell-
mediated immune response
 Clinical immunology
Clinical immunology is the study of diseases caused by disorders of the
immune system (failure, aberrant action, and malignant growth of the
cellular elements of the system). It also involves diseases of other
systems, where immune reactions play a part in the pathology and
clinical features.
The diseases caused by disorders of the immune system fall into two
broad categories:
• immunodeficiency, in which parts of the immune system fail to provide
an adequate response (examples include chronic granulomatous disease
and primary immune diseases);
• autoimmunity, in which the immune system attacks its own host's body
(examples include systemic lupus erythematosus, rheumatoid
arthritis, Hashimoto's disease andmyasthenia gravis).
Other immune system disorders include various hypersensitivities (such
as in asthma and other allergies) that respond inappropriately to
otherwise harmless compounds.
 Developmental immunology
• The body’s capability to react to antigen depends on a person's
age, antigen type, maternal factors and the area where the
antigen is presented. 
• Neonates are said to be in a state of physiological
immunodeficiency, because both their innate and adaptive
immunological responses are greatly suppressed. Once born, a
child’s immune system responds favorably to protein antigens
while not as well to glycoproteins and polysaccharides.
• In fact, many of the infections acquired by neonates are caused
by low virulence organisms
like Staphylococcus and Pseudomonas.
• In neonates, opsonic activity and the ability to activate
the complement cascade is very limited
• For example, the mean level of C3 in a newborn is approximately
65% of that found in the adult
• Phagocytic activity is also greatly impaired in newborns.
• This is due to lower opsonic activity, as well as diminished up-
regulation of integrin and selectin receptors, which limit the ability
of neutrophils to interact with adhesion molecules in the endothelium.
• Their monocytes are slow and have a reduced ATP production, which also
limits the newborn's phagocytic activity. Although, the number of
total lymphocytes is significantly higher than in adults, the cellular and
humoral immunity is also impaired. 
• Antigen-presenting cells in newborns have a reduced capability to activate
T cells. Also, T cells of a newborn proliferate poorly and produce very small
amounts of cytokines like IL-2, IL-4, IL-5, IL-12, and IFN-g which limits their
capacity to activate the humoral response as well as the phagocitic activity of
macrophage.
• B cells develop early during gestation but are not fully active.

Artist's impression of monocytes

• Maternal factors also play a role in the body’s immune response.
• At birth, most of the immunoglobulin present is maternal IgG. Because IgM,
IgD, IgE and IgA don’t cross the placenta, they are almost undetectable at
birth. Some IgA is provided by breast milk.
• These passively-acquired antibodies can protect the newborn for up to 18
months, but their response is usually short-lived and of low affinity.
• These antibodies can also produce a negative response. If a child is exposed to
the antibody for a particular antigen before being exposed to the antigen itself
then the child will produce a dampened response. 
• Passively acquired maternal antibodies can suppress the antibody response to
active immunization.
• Similarly the response of T-cells to vaccination differs in children compared to
adults, and vaccines that induce Th1 responses in adults do not readily elicit
these same responses in neonates.
• Between six and nine months after birth, a child’s immune system begins to
respond more strongly to glycoproteins, but there is usually no marked
improvement in their response to polysaccharides until they are at least one
year old.
• This can be the reason for distinct time frames found in vaccination schedules.
• During adolescence, the human body undergoes various physical,
physiological and immunological changes triggered and mediated
by hormones, of which the most significant in females is 17-β-
oestradiol (an oestrogen) and, in males, is testosterone.
• Oestradiol usually begins to act around the age of 10 and testosterone some
months later. There is evidence that these steroids act directly not only on
the primary and secondary sexual characteristics but also have an effect on
the development and regulation of the immune system, including an
increased risk in developing pubescent and post-pubescent
autoimmunity. There is also some evidence that cell surface receptors on B
cells and macrophages may detect sex hormones in the system.
• The female sex hormone 17-β-oestradiol has been shown to regulate the
level of immunological response, while some male androgens such as
testosterone seem to suppress the stress response to infection. Other
androgens, however, such as DHEA, increase immune response. 
• As in females, the male sex hormones seem to have more control of the
immune system during puberty and post-puberty than during the rest of a
male's adult life.
• Physical changes during puberty such as thymic involution also affect
immunological response
 Immunotherapy
• The use of immune system components to treat a disease
or disorder is known as immunotherapy.
• Immunotherapy is most commonly used in the context of
the treatment of cancers together
with chemotherapy (drugs) and radiotherapy 
(radiation).
• However, immunotherapy is also often used in the
immunosuppressed (such as HIV patients) and people
suffering from other immune deficiencies or autoimmune
diseases.
• This includes regulating factors such as IL-2, IL-10, GM-CSF
B, IFN-α.
 Diagnostic immunology
• The specificity of the bond between antibody and antigen
has made the antibody an excellent tool for the detection
of substances by a variety of diagnostic techniques.
• Antibodies specific for a desired antigen can be conjugated
with an isotopic (radio) or fluorescent label or with a color-
forming enzyme in order to detect it.
• However, the similarity between some antigens can lead
to false positives and other errors in such tests by
antibodies cross-reacting with antigens that aren't exact
matches.
 Antibody

Each antibody binds to a specific antigen; an interaction similar to a lock and key.

• An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-
shaped protein produced mainly by plasma cells that is used by the immune
system to identify and neutralize pathogens such as bacteria and viruses.
• The antibody recognizes a unique molecule of the harmful agent, called
an antigen, via the Fab's variable region.
• Each tip of the "Y" of an antibody contains aparatope (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).
• Depending on the antigen, the binding may impede the biological process
causing the disease or may activate macrophages to destroy the foreign
substance.
• The ability of an antibody to communicate with the other components of the
immune system is mediated via its Fc region (located at the base of the "Y"),
which contains a conservedglycosylation site involved in these interactions. The
production of antibodies is the main function of the humoral immune system.
• Antibodies are secreted by B cells of the adaptive immune
system, mostly by differentiated B cells called plasma cells.
• Antibodies can occur in two physical forms, a soluble form that is
secreted from the cell to be free in the blood plasma, 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 found only 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. 
• In most cases, interaction of the B cell with a T helper cell is
necessary to produce full activation of the B cell and, therefore,
antibody generation following antigen binding. 
• Soluble antibodies are released into the blood and tissue fluids,
as well as many secretions to continue to survey for invading
microorganisms.
• Antibodies are glycoproteins belonging to the immunoglobulin superfamily.
• They constitute most of the gamma globulin fraction of the blood proteins.
• They are typically made of basic structural units—each with two large heavy
chains and two small light chains. There are several different types of
antibody heavy chains that define the five different types of crystallisable
fragments (Fc) that may be attached to the antigen-binding fragments. The
five different types of Fc regions allow antibodies to be grouped into
five isotypes.
• Each Fc region of a particular antibody isotype is able to bind to its specific Fc
Receptor (except for IgD, which is essentially the BCR), thus allowing the
antigen-antibody complex to mediate different roles depending on which FcR
it binds. The ability of an antibody to bind to its corresponding FcR is further
modulated by the structure of the glycan(s) present at conserved sites within
its Fc region. 
• The ability of antibodies to bind to FcRs helps to direct the appropriate
immune response for each different type of foreign object they encounter. 
• For example, IgE is responsible for an allergic response consisting of mast
cell degranulation and histamine release. IgE's Fab paratope binds to
allergic antigen, for example house dust mite particles, while its Fc region
binds to Fc receptor ε. The allergen-IgE-FcRε interaction mediates allergic
signal transduction to induce conditions such as asthma.
 Forms
• The membrane-bound form of an antibody may be called a surface
immunoglobulin (sIg) or a membrane immunoglobulin (mIg).
• It is part of the B cell receptor (BCR), which allows a B cell to detect when
a specific antigen is present in the body and triggers B cell activation. 
• The BCR is composed of surface-bound IgD or IgM antibodies and
associated Ig-α and Ig-β heterodimers, which are capable of signal
transduction. 
• A typical human B cell will have 50,000 to 100,000 antibodies bound to
its surface. 
• Upon antigen binding, they cluster in large patches, which can exceed 1
micrometer in diameter, on lipid rafts that isolate the BCRs from most
other cell signaling receptors.
• These patches may improve the efficiency of the cellular immune
response.
• In humans, the cell surface is bare around the B cell receptors for several
hundred nanometers, which further isolates the BCRs from competing
influences.
 Isotypes
• Antibodies can come in different varieties known as isotypes or
classes.
• In placental mammals there are five antibody isotypes known as
IgA, IgD, IgE, IgG, and IgM.
• They are each named with an "Ig" prefix that stands for
immunoglobulin, a name sometimes used interchangeably with
antibody, and differ in their biological properties, functional
locations and ability to deal with different antigens, as depicted
in the table. 
• The different suffixes of the antibody isotypes denote the
different types of heavy chains the antibody contains, with each
heavy chain class named alphabetically: α (alpha), γ (gamma), δ
(delta), ε (epsilon), and μ (mu). This gives rise to IgA, IgG, IgD,
IgE, and IgM, respectively.
 Structure
• Antibodies are heavy (~150 kDa) globular plasma proteins. They have sugar chains
(glycans) added to conserved amino acid residues. 
• In other words, antibodies areglycoproteins. 
• The attached glycans are critically important to the structure and function of the
antibody. Among other things the expressed glycans can modulate an antibody's affinity
for its corresponding FcR(s).
• The basic functional unit of each antibody is an immunoglobulin (Ig) monomer (containing
only one Ig unit); secreted antibodies can also be dimeric with two Ig units as with IgA,
tetrameric with four Ig units like teleost fish IgM, or pentameric with five Ig units, like
mammalian IgM
 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 and are
classified into different categories (for example, variable or IgV,
and constant or IgC) according to their size and function.
• They have a characteristic immunoglobulin fold in which two beta
sheets create a "sandwich" shape, held together by interactions
between conserved cysteines and other charged amino acids.
• Each heavy chain has two regions, the constant region and
the variable region.
• The constant region is identical in all antibodies of the
same isotype, but differs in antibodies of different
isotypes. Heavy chains γ, α and δ have a constant region
composed of three tandem (in a line) Ig domains, and a
hinge region for added flexibility; heavy chains μ and ε
have a constant region composed of fourimmunoglobulin
domains.
• The variable region of the heavy chain differs in antibodies
produced by different B cells, but is the same for all
antibodies produced by a single B cell or B cell clone.
• The variable region of each heavy chain is approximately
110 amino acids long and is composed of a single Ig
domain.
 The main categories of antibody action include the
following:

• Neutralisation, in which neutralizing antibodies block parts of

the surface of a bacterial cell or virion to render its attack
ineffective
• Agglutination, in which antibodies "glue together" foreign cells
into clumps that are attractive targets for phagocytosis
• Precipitation, in which antibodies "glue together" serum-
soluble antigens, forcing them to precipitate out of solution in
clumps that are attractive targets for phagocytosis
• Complement activation (fixation), in which antibodies that are
latched onto a foreign cell encourage complement to attack it
with a membrane attack complex, which leads to the
following:
– Lysis of the foreign cell
– Encouragement of inflammation by chemotactically attracting
 Activation of complement
• Antibodies that bind to surface antigens (for example, on
bacteria) will attract the first component of the complement
cascade with their Fc region and initiate activation of the
"classical" complement system.
• This results in the killing of bacteria in two ways.
• First, the binding of the antibody and complement molecules
marks the microbe for ingestion by phagocytes in a process
called opsonization these phagocytes are attracted by certain
complement molecules generated in the complement cascade.
• Second, some complement system components form
a membrane attack complex to assist antibodies to kill the
bacterium directly (bacteriolysis)
 Immunoglobulin diversity
• Virtually all microbes can trigger an antibody response.
• Successful recognition and eradication of many different types
of microbes requires diversity among antibodies; their amino
acid composition varies allowing them to interact with many
different antigens.
• It has been estimated that humans generate about 10 billion
different antibodies, each capable of binding a distinct epitope
of an antigen.
• Although a huge repertoire of different antibodies is generated
in a single individual, the number of genes available to make
these proteins is limited by the size of the human genome.
• Several complex genetic mechanisms have evolved that allow
vertebrate B cells to generate a diverse pool of antibodies from
a relatively small number of antibody genes
Antibody antigen complex
 Immunoglobulin G
• Immunoglobulin G (IgG) is a type of antibody. It is a protein
complex composed of four peptide chains—two identical heavy
chains and two identical light chains arranged in a Y-shape typical of
antibody monomers.
• Each IgG has two antigen binding sites.
• Representing approximately 75% of serum antibodies in humans,
IgG is the most common type of antibody found in the circulation. 
• IgG molecules are created and released by plasma B cells.
• IgG is the main type of antibody found in blood and extracellular
fluid allowing it to control infection of body tissues.
• By binding many kinds of pathogens such as viruses, bacteria,
and fungi, IgG protects the body from infection
• It is the only isotype that has receptors to facilitate passage
through the human placenta
• IgG-mediated binding of pathogens causes their immobilization
and binding together via agglutination; IgG coating of pathogen
surfaces (known as opsonization) allows their recognition and
ingestion by phagocytic immune cells leading to the elimination
of the pathogen itself;
• IgG activates the classical pathway of the complement system, a
cascade of immune protein production that results in pathogen
elimination;
• IgG also binds and neutralizes toxins;
• IgG also plays an important role in antibody-dependent cell-
mediated cytotoxicity (ADCC) and intracellular antibody-
mediated proteolysis, in which it binds to TRIM21 (the receptor
with greatest affinity to IgG in humans) in order to direct marked
virions to the proteasome in the cytosol.;
• IgG is also associated with type II and type
III hypersensitivity reactions.
 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.

Schematic diagram of the basic unit of immunoglobulin (antibody) Fab Fc

heavy chain (consist of VH, CH1, hinge, CH2 and CH3 regions: from N-term)
light chain (consist of VL and CL regions: from N-term) antigen binding site
hinge regions (*) -S-S- mean disulfide bonds.
• The various regions and domains of a typical IgG
 Immunoglobulin A

The dimeric IgA molecule
1 H-chain
2 L-chain
3 J-chain
4 secretory component
• Immunoglobulin A (IgA, also referred to as sIgA) is an antibody that plays a
critical role in immune function in the mucous membranes.
• More IgA is produced in mucosal linings than all other types of antibody
combined; between three and five grams are secreted into the
intestinal lumen each day. 
• This accumulates up to 15% of the total immunoglobulin produced in the entire
body.
• IgA has two subclasses (IgA1 and IgA2) and can exist in a dimeric form
called secretory IgA (sIgA).
• In its secretory form, IgA is the mainimmunoglobulin found in mucous
secretions, including tears, saliva, sweat, colostrum and secretions from
the genitourinary tract,gastrointestina tract, prostate and respiratory epithelium.
• It is also found in small amounts in blood.
• The secretory component of sIgA protects the immunoglobulin from being
degraded by proteolytic enzymes, thus sIgA can survive in the
harsh gastrointestinal tract environment and provide protection
against microbes that multiply in body secretions. 
• sIgA can also inhibit inflammatory effects of other immunoglobulins. 
• IgA is a poor activator of the complement system, and opsonises only weakly.
Its heavy chains are of the type α.
Immunoglobulin E
The role of mast cells in the development of allergy.
• Immunoglobulin E (IgE) is a kind of antibody (or immunoglobulin (Ig)
"isotype") that has only been found in mammals
• IgE is synthesised by plasma cells.
• Monomers of IgE consist of two heavy chains (ε chain) and two light
chains, with the ε chain containing 4 Ig-like constant domains (Cε1-
Cε4). 
• IgE's main function is immunity to parasites such as helminths
like Schistosoma mansoni, Trichinella spiralis, and Fasciola hepatica.
• IgE is utilized during immune defense against
certain protozoan parasites such as Plasmodium falciparum.
• IgE also has an essential role in type I hypersensitivity, which
manifests various allergic diseases, such as allergic asthma, most
types of sinusitis, allergic rhinitis, food allergies, and specific types
of chronic urticaria and atopic dermatitis.
• IgE also plays a pivotal role in responses to allergens, such
as: anaphylactic drugs, bee stings, and antigen preparations used in
desensitization immunotherapy.
• Degranulation processes 1 - antigen; 2 - IgE antibody; 3 - FcεRI
receptor; 4 - preformed mediators (histamine, proteases,
chemokines, heparin); 5 - granules; 6 - mast cell; 7 - newly formed
mediators (prostaglandins, leukotrienes, thromboxanes, PAF)
• IgE also has an essential role in type I hypersensitivity, which
manifests various allergic diseases, such as allergic asthma,
most types of sinusitis, allergic rhinitis, food allergies, and
specific types of chronic urticaria and atopic dermatitis.
• IgE also plays a pivotal role in responses to allergens, such
as: anaphylactic drugs, bee stings, and antigen preparations
used in desensitization immunotherapy.
• Although IgE is typically the least abundant isotype—blood
serum IgE levels in a normal ("non-atopic") individual are
only 0.05% of the Ig concentration, compared to 75% for
the IgGs at 10 mg/ml, which are the isotypes responsible for
most of the classical adaptive immune response—it is
capable of triggering the most powerful inflammatory
reactions.
• There is much speculation into what physiological benefits IgE
contributes, and, so far, circumstantial evidence in animal models and
statistical population trends have hinted that IgE may be beneficial in
fighting gut parasites such as Schistosoma mansoni, but this has not
been conclusively proven in humans.
• Epidemiological research shows that IgE level is increased when infected
by Schistosoma mansoni,  Necator americanus, and nematodes in
human.
• It is most likely beneficial in removal of hookworms from the lung.
• Although it is not yet well understood, IgE may play an important role in
the immune system’s recognition of cancer, in which the stimulation of a
strong cytotoxic response against cells displaying only small amounts of
early cancer markers would be beneficial.
• If this were the case, anti-IgE treatments such as omalizumab (for
allergies) might have some undesirable side effects.
• However, a recent study, which was performed based on pooled analysis
using comprehensive data from 67 phase I to IV clinical trials of
omalizumab in various indications, concluded that a causal relationship
between omalizumab therapy and malignancy is unlikely
 Immunoglobulin M

• IgM (Immunoglobulin M) antibody molecule consisting of 5 base units.

1: Base unit.
2: Heavy chains.
3: Light chains.
4: J chain.
5: Intermolecular disulfide bonds.
• Immunoglobulin M, or IgM for short, is a
basic antibody that is produced by B cells.
• IgM is by far the physically largest antibody in
the human circulatory system. It is the first
antibody to appear in response to initial
exposure to an antigen. 
• The spleen, where plasmablasts responsible
for antibody production reside, is the major
site of specific IgM production.
 Structure and function
• IgM forms polymers where multiple immunoglobulins are covalently linked
together with disulfide bonds, mostly as a pentamer but also as a hexamer.
IgM has a molecular mass of approximately 970 kDa (in its pentamer
form). Because each monomer has two antigen binding sites, a pentameric
IgM has 10 binding sites.
• Typically, however, IgM cannot bind 10 antigens at the same time because the
large size of most antigens hinders binding to nearby sites.
• IgM antibodies appear early in the course of an infection and usually reappear,
to a lesser extent, after further exposure. IgM antibodies do not pass across
the human placenta (only isotype IgG).
• These two biological properties of IgM make it useful in the diagnosis of
infectious diseases.
• Demonstrating IgM antibodies in a patient's serum indicates recent infection,
or in a neonate's serum indicates intrauterine infection (e.g. congenital rubella
syndrome).
• The development of anti-donor IgM after organ transplantation is not
associated with graft rejection but it may have a protective effect
 B cell
• B cells, also known as B lymphocytes, are a type of white blood cell of
the lymphocyte subtype.
• They function in the humoral immunity component of the adaptive immune
system by secreting antibodies. 
• Additionally, B cells present antigen (they are also classified as
professional antigen-presenting cells (APCs)) and secrete cytokines.
• In mammals, B cells mature in the bone marrow, which is at the core of
most bones.  In birds, B cells mature in the bursa of Fabricius, a lymphoid
organ. (The "B" from B cells comes from the name of this organ, where it was
first discovered by Chang and Glick, and not from bone marrow as commonly
believed).
• B cells, unlike the other two classes of lymphocytes,  T
cells and natural killer cells, express B cell receptors (BCRs) on their cell
membrane.
• BCRs allow the B cell to bind a specific antigen, against which it will initiate an
antibody response.
• Basic B cell function: bind an antigen, receive help from a
cognate helper T cell, and differentiate into a plasma cell that
secretes large amounts of antibodies
 Hematopoietic stem cell
• Hematopoietic stem cells (HSCs) or hemocytoblasts are the stem cells that
give rise to all the other blood cells through the process of haematopoiesis.
• They are derived from mesoderm and located in the red bone marrow,
which is contained in the core of most bones.
• They give rise to both the myeloid and lymphoid lineages of blood cells.
( Myeloid cells
include monocytes, macrophages, neutrophils,basophils, eosinophils, eryth
rocytes, dendritic cells, and megakaryocytes or platelets. Lymphoid cells
include T cells, B cells, andnatural killer cells.)
• The definition of hematopoietic stem cells has evolved since HSCs were
first discovered in 1961. 
• The hematopoietic tissue contains cells with long-term and short-term
regeneration capacities and committed multipotent, oligopotent,
and unipotent progenitors. HSCs constitute 1:10.000 of cells in myeloid
tissue.
• Sketch of bone marrow and its cells
• Plasma cells, also called plasma B
cells, plasmocytes, plasmacytes, or effector B cells,
are white blood cells that secrete large volumes
of antibodies.
• They are transported by the blood plasma and
the lymphatic system.
• Plasma cells originate in the bone marrow; 
• B cells differentiate into plasma cells that produce
antibody molecules closely modeled after the receptors of
the precursor B cell.
• Once released into the blood and lymph, these antibody
molecules bind to the target antigen (foreign substance)
and initiate its neutralization or destruction
Thanks bro