SEMINAR REPORT ON

ANTIGEN-ANTIBODY
INTERACTIONS
SUBMITTED BY:
SOUMYA SUDESHNA
BSc. ZOOLOGY HONOURS
UNIVERSITY ROLL NO:- 1602010890180003
 Antibodies and antigen

 Antibodies are population of glycoproteins that are synthesized and

secreted by plasma cells(activated B lymphocytes) in response to a
foreign macromolecule, called an antigen(immunogen).
 The paratopes (antigen-binding sites) of antibodies bind specifically to
the corresponding epitopes(antigenic determinants) of an antigen or
pathogen. Such binding results in the formation of antigen-antibody
(Ag-Ab)complexes which initiate a variety of immune response for
successful elimination of antigen or pathogen.
 The specific interaction between antigen(Ag) and antibody(Ab) is
called antigen-antibody interaction or in short Ag-Ab interaction.
 General characteristics of Ag-Ab
interactions
NATURE OF ANTIGEN-ANTIBODY REACTIONS
Lock and Key Concept
The combining site of an antibody is located in the Fab portion of the molecule and is
constructed from the hypervariable regions of the heavy and light chains. X-Ray
crystallography studies of antigen-antibody interactions show that the antigenic
determinant nestles in a cleft formed by the combining site of the antibody as
illustrated in Figure 1. Thus, our concept of antigen-antibody reactions is one of a key
(i.e. the antigen) which fits into a lock (i.e. the antibody).

Non-covalent Bonds
The bonds that hold the antigen to the antibody combining site are all non-covalent in
nature. These include hydrogen bonds, electrostatic bonds, Van der Waals forces and
hydrophobic bonds. Multiple bonding between the antigen and the antibody ensures
that the antigen will be bound tightly to the antibody.
Reversibility
Since antigen-antibody reactions occur via non-covalent bonds, they are by their nature
reversible.
AFFINITY AND AVIDITY
Affinity
Antibody affinity is the strength of the reaction between a single antigenic determinant
and a single combining site on the antibody. It is the sum of the attractive and repulsive
forces operating between the antigenic determinant and the combining site of the
antibody as illustrated in Figure 2.
Affinity is the equilibrium constant that describes the antigen-antibody reaction as
illustrated in Figure 3. Most antibodies have a high affinity for their antigens.
Avidity
Avidity is a measure of the overall strength of binding of an antigen with many antigenic
determinants and multivalent antibodies. Avidity is influenced by both the valence of the
antibody and the valence of the antigen. Avidity is more than the sum of the individual
affinities. This is illustrated in Figure 4.
To repeat, affinity refers to the strength of binding between a single antigenic determinant
and an individual antibody combining site whereas avidity refers to the overall strength of
binding between multivalent antigens and antibodies.
SPECIFICITY AND CROSS REACTIVITY
Specificity
Specificity refers to the ability of an individual antibody combining site to react with
only one antigenic determinant or the ability of a population of antibody molecules to
react with only one antigen. In general, there is a high degree of specificity in antigen-
antibody reactions. Antibodies can distinguish differences in:
 The primary structure of an antigen
 Isomeric forms of an antigen
 Secondary and tertiary structure of an antigen
Cross reactivity
Cross reactivity refers to the ability of an individual antibody combining site to react
with more than one antigenic determinant or the ability of a population of antibody
molecules to react with more than one antigen. Figure 5 illustrates how cross reactions
can arise. Cross reactions arise because the cross reacting antigen shares an epitope
in common with the immunizing antigen or because it has an epitope which is
structurally similar to one on the immunizing antigen (multispecificity).
 Types of Antigen-Antibody interaction

 Precipitation Reaction:
 The interaction between an antibody and a soluble antigen in aqueous solution
forms a lattice which ultimately develops a visible precipitate. Antibodies which
can aggregate soluble antigens are designated as precipitins. It requires a time to
develop a precipitate. The precipitate, attaining insolubility due to formation of
ionic bond with antigen-antibody molecules, helps to lose its charge.
 Ag-Ab lattice formation depends on the valency of both the antigen and the
antibody, in this respect:
 I. The antibody must be bivalent; a precipitate will not form with monovalent F(ab)
fragments.
 ii. The antigen must either be bivalent or polyvalent; it must have at-least two
copies of the same epitope or have different epitopes that react with different
antibodies present in polyclonal antisera (Fig. 5.5 and 5.6).
Agglutination reactions
The interaction between antibody and a particulate antigen results in visible clumping
called agglutination. Antibodies that produce such reactions are called agglutinins.
Better agglutination takes place with IgM antibody than with IgG antibodies. Excess of
an antibody also inhibits agglutination reaction; this inhibition is called prozone
phenomenon.
1.Agglutination is more sensitive than precipitation for the detection of antibodies.
2.Agglutination occurs optimally when antigens and antibodies react in equivalent
proportions.
The prozone phenomenon may be seen when either an antibody or an antigen is in
excess. Incomplete or monovalent antibodies do not cause agglutination, though they
combine with the antigen. They may act as blocking antibodies, inhibiting agglutination
by the complete antibody added subsequently.

Types of agglutination
1.Slide agglutination: Serotyping.
2.Tube agglutination: e.g. Widal test.
3. Indirect (passive agglutination): where soluble antigens are coated on vehicle
particle e.g. latex particle, RBCs.
How to perform slide agglutination
Beneficial Effects of Ag-Ab interactions

 Neutralization in the immunological sense refers to the ability of specific

antibodies to block the site(s) on viruses that they use to enter their target
cell. The effect of a neutralizing antibody can be negligible even with large
excesses of antibody production if they lack specificity to this antigen. The
production of specific antibodies can be learned for a faster response at
next exposition.
 The reduction or destruction of a homologous infectious agent can be
partial or complete and can make it no longer infectious or pathogenic to
other cells
 Antibody opsonization is the process by which the pathogen is marked
for ingestion and eliminated by the phagocytes.
Given normal inflammatory circumstances, microbial pathogen-associated molecular patterns
(PAMPs) bind with the endocytic pattern recognition receptors (PRRs) of phagocytes, which
mediates neutrophil mediation or macrophage phagocytosis. As well as endocytic PRRs,
phagocytes furthermore express opsonin receptors such as Fc receptor and complement receptor
1 (CR1). Should the microbe be coated with opsonizing antibodies or C3b complement, the co-
stimulation of endocytic PRR and opsonin receptor increases the efficacy of the phagocytic
process, enhancing the lysosomal elimination of the infective agent. This mechanism of antibody-
mediated increase in phagocytic efficacy is named opsonization.
Opsonization involves the binding of an opsonin, e.g., antibody, to an epitope on a pathogen.[1]
After opsonin binds to the membrane, phagocytes are attracted to the pathogen. The Fab
portion of the antibody binds to the antigen, whereas the Fc portion of the antibody binds to an
Fc receptor on the phagocyte, facilitating phagocytosis. The core receptor + opsonin complex
also creates byproducts like C3b and C4b which are important components for the efficient
function of the complement system. These components are deposited on the cell surface of the
pathogen and aid in its destruction.
The cell can also be destroyed by a process called antibody-dependent cell-mediated
cytotoxicity, in which the pathogen does not need to be phagocytosed to be destroyed. During
this process, the pathogen is opsonized and bound with the antibody IgG via its Fab domain. This
allows the antibody binding of an immune effector cell via its Fc domain. Antibody-dependent
cell-mediated inherent mediation then triggers a release of lysis products from the bound immune
effector cell (monocytes, neutrophils, eosinophils and NK cells). Lack of mediation can cause
inflammation of surrounding tissues and damage to healthy cells.
1) Antibodies (A) and pathogens (B) free roam in the blood. 2) The antibodies bind to pathogens, and can
do so in different formations such as: opsonization (2a), neutralization (2b), and agglutination (2c). 3) A
phagocyte (C) approaches the pathogen, and Fc region (D) of the antibody binds to one of the Fc
receptors (E) on the phagocyte. 4) Phagocytosis occurs as the pathogen is ingested.
Harmful effects of Ag-Ab interactions

 Auto-immune diseases
 Hypersensitivity
 Rheumatic fever
 Erythroblastosisfoetalis
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