LEAD CITY UNIVERSITY

OYO STATE, IBADAN

DEPARTMENT OF MEDICAL LABORATORY SCIENCE

BLOOD GROUP SEROLOGY (MLS 318) TERM PAPER

LEVEL 300

TOPIC: IgG and IgM antibodies

PRESENTED BY GROUP 8

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MEMBERS
1.Olorunfemi Bolorunduro Deborah LCU/UG/19/15408
2.Yusuf Olabisi Grace LCU/UG/19/14405
3. Raheem Rashidat Abiola LCU/UG/20/16289
4. Oguntade Bright Adesoji LCU/UG/19/15810
5. Akinsete Anuoluwapo Idowu LCU/UG/19/14439
6. Musa Maryam LCU/UG/19/15827
7. Akinnola oluwatobiloba Opeoluwa LCU/UG/20/16578
8. Nnakwe Rebecca Ijeoma LCU/UG/19/16038
9. Taiwo Oluwadamilola Sarah LCU/UG/19/14528
10.Agbaje Boluwatife temilade LCU/UG/19/14563
11. Egbekai Vivian Nina LCU/UG/19/14778
12.Ipadeola Joy Ruth LCU/UG/19/15143

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 INTRODUCTION

Immunoglobulins (Ig) or antibodies are glycoproteins that are produced in

response to foreign substances entering the living body. Beta cells are instructed
by specific immunogens, for example, bacterial proteins, to differentiate into
plasma cells, which are protein-making cells that participate in humoral immune
responses against bacteria, viruses, fungi, parasites, cellular antigens, chemicals,
and synthetic substances. They (antibodies) bind to them (antigens or
immunogens) to form antigen-antibody complexes resulting in Ag elimination
and protection of the body of the host.

The immunogen or antigen reacts with a B-cell receptor (BCR) on the cell
surface of B lymphocytes, and a signal is produced that directs the activation of
transcription factors to stimulate the synthesis of antibodies, which are highly
specific for the immunogen that stimulated the B cell. Furthermore, one clone of
B cell makes an immunoglobulin (specificity). Besides, the immune system
remembers the antigens that caused a previous reaction (memory) due to the
development of memory B cells. These are intermediate, differentiated B cells
with the capability to quickly become plasma cells. Circulating antibodies
recognize antigen in tissue fluids and serum.

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 GENERAL FUNCTIONS

Antigens binding- Immunoglobulins bind to specific Antigenic determinants

(AD) on an antigen. They bind to at least 2 or in a few cases more Ads which
are closely related and the number of ADs an antibody can bind to is referred to
as its valency.

Most Immunoglobulins mediate several effector functions which include

fixation of complement that results to lyses of cells and release of biologically
active molecules, binding of various cells to facilitate specific functions by
bound cells e.g., phagocytic cells lymphocytes, platelets etc. Most effector
functions of Abs are carried out after the Ab binds to antigens. Different
immunoglobulins molecules can have different antigen binding properties
because of different VH and VL regions.

TYPES IMMUNOGLOBULIN
I. IMMUNOGLOBULIN M (IgM)
IgM has a molecular weight of 970 Kd and average serum concentration
of 1.5 mg/ml. It is mainly produced in the primary immune response to
infectious agents or antigens. It is a pentamer and activates the classical
pathway of the complement system. IgM is regarded as a potent
agglutinin (e.g., anti-A and anti-B isoagglutinin present in type B and
type A blood respectively) and a monomer of IgM is used as a B cell
receptor (BCR).
II. IMMUNOGLOBULIN G (IgG)

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 IgG is a monomer with an approximate molecular weight of 146 Kd and a
serum concentration of 9.0 mg/mL. It is synthesized mostly in the
secondary immune response to pathogens. IgG can activate the classical
pathway of the complement system, and it also is highly protective. The
four subclasses of IgG include IgG1, IgG2, IgG3, and IgG4. IgG crosses
the placentae, protecting the neonate from infectious diseases.

BASIC STRUCTURE OF IMMUNOGLOBULINS

All Immunoglobulins have the same basic structural units of 2 identical light
chains and 2 identical heavy chains, the heavy and light chains are joined
together by interchain disulphide bonds and non-covalent interactions. The
number of interchain disulphide bonds varies among different
Immunoglobulins. Amino acid sequence of both heavy and light chains of an
Immunoglobulin (Ig) characterizes two distinct regions of the chains based on
variability of the amino acid sequence, known as VARIABLE (V) and
CONSTANT (C) regions .Light and heavy chains are composed of both a
variable and constant region designated VL and CL (light chains) and VH and
CH (heavy chains).The amino acid sequence of the variable region form the N-
terminal ends of the chains and determine antigenic specificity of the
Immunoglobulins. Constant regions are the same for each specific class of Ig
and carry the effector sites

IMMUNOGLOBULIN M
IgM is the first immunoglobulin expressed during B cell development. IgM antibodies are
associated with a primary immune response and are frequently used to diagnose acute
exposure to an immunogen or pathogen.
Immunoglobulin M (IgM) is one of several isotypes of antibody (also known
as immunoglobulin) that are produced by vertebrates. IgM is the largest antibody, and it is the

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first antibody to appear in the response to initial exposure to an antigen. In the case of
humans and other mammals that have been studied, the spleen, where Plasmablasts that are
responsible for antibody production reside, is the major site of specific IgM production

Structure of immunoglobulin monomer

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Structure of Immunoglobulin M

SIGNIFICANCE OF IGM ANTIBODIES IN VARIOUS DISEASE STATES

Infection
During infection and exposure to foreign antigens, IgM antibodies represent the
first immunoglobulin produced and act as the first adaptive defence to protect
the body. Therefore, the detection of serum IgM antibody is a potential method
for early diagnosis. Because of falsepositive reactions, other tests should be
performed for confirmation. For example, by evaluating both IgM and IgG
antibody production (IgM–IgG antibody combined screening) as a diagnostic
method for viral infection, specificity can be increased with higher sensitivity.
Additionally, this test reveals whether the current infection is an initial infection
or reinfection. For example, IgM positivity and IgG negativity indicate a recent

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primary infection, whereas IgM negativity and IgG positivity suggest
subsequent reinfection.

Autoimmunity
Serum IgM antibodies against double-stranded DNA are more likely to be
detected during inactive SLE than during active SLE. Serum IgM antibodies are
detected more often in other sclerodermas, collagen diseases, chronic hepatitis,
and infectious mononucleosis Pathogens than in SLE. Although their specificity
is low, these antibodies are associated with pathological conditions, and their
levels tend to be lower during the active phase in follow-up observations in
patients with SLE. Thus, clinical evaluation of both IgG and IgM autoantibodies
is useful for the detailed evaluation of pathological conditions in the field of
autoimmunity.

Cancer
In breast cancer, the detection of autoantibodies against tumor-associated
antigens is expected to be useful for early diagnosis and prognosis, and IgG
antibody-like molecules have been proposed as indices of therapeutic efficacy.
However, IgG antibodies are usually subject to immunoregulation, and they
reflect the suppression of the immune response against tumors. Conversely,
natural IgM antibodies contribute to tumor elimination by directly presenting
tumor antigen to NK cells and DCs. Natural IgM antibodies perform
neutralization by directly binding to tumor cells, and they activate B cells via T
cell activation. Therefore, the detection of IgM antibodies is expected to be
useful as an early diagnostic method in combination with imaging analyses.

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IMMUNOGLOBULIN G
IgG is the predominant isotype found in the body. It has the longest serum half-
life of all immunoglobulin isotypes. It is also the most extensively studied class
of immunoglobulins.

STRUCTURE
IgG antibodies are large globular proteins with a molecular weight of about 150
kDa made of four peptide chains.

Structure of Immunoglobulin G

SUBCLASSES OF IMMUNOGLOBULIN G
There are four IgG subclasses (IgG1, 2, 3, and 4) in humans, named in order of
their abundance in serum (IgG1 being the most abundant). Subclasses IgG1,

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IgG2, IgG3, and IgG4 are differentiated based on the size of the hinge region,
position of interchain disulphide bonds, and molecular weight. The subclasses
also differ in their ability to activate complement:

I. IgG1
It comprises 60 to 65% of the total main subclass IgG. It is involved in
opsonization and activation of the complement cascade. A deficiency in
IgG1 isotype is typically a sign of a hypogammaglobulinemia.

II. IgG2
It comprises 20 to 25% of the main subclass and is the prevalent immune
response against carbohydrate/polysaccharide antigens. Among all IgG
isotype deficiencies, a deficiency in IgG2 is the most common and is
associated with recurring airway/respiratory infections in infants.

III. IgG3
IgG3 comprises around 5 to 10% of total IgG and plays a major role in
the immune responses against protein or polypeptide antigens.

IV. IgG4
Comprising usually less than 4% of total IgG, IgG4 does not bind to
polysaccharides. Recent studies have shown that elevated serum levels of
IgG4 are found in patients suffering from sclerosing pancreatitis,
cholangitis and interstitial pneumonia caused by infiltrating IgG4 positive
plasma cells. The precise role of IgG4 is still mostly unknown.

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FUNCTIONS OF IMMUNOGLOBULIN G
IgG is the main type of antibody found in blood and extracellular fluid allowing
it to control infection of body tissues.
IgG is the only class of immunoglobulin that can cross the placenta in humans,
and it is largely responsible for protection of the newborn during the first
months of life.
IgG is the major immunoglobulin in blood, lymph fluid, cerebrospinal fluid and
peritoneal fluid and a key player in the humoral immune response.
IgG is produced in a delayed response to an infection and can be retained in the
body for a long time. The longevity in serum makes IgG most useful for passive
immunization by transfer of this antibody. Detection of IgG usually indicates a
prior infection or vaccination.
Because of its relative abundance and excellent specificity toward antigens, IgG
is the principal antibody used in immunological research and clinical
diagnostics.

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CONCLUSION
Ig is the most used blood product in clinical practice. Over the years, there has
been considerable progress in its production from the processing of plasma, The
mechanisms of action of Ig are multiple and go far beyond simply blocking Fc
receptors of phagocytes. It is believed that many mechanisms are yet to be
clarified and will certainly contribute to better clinical indications of this blood
product.

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