Generally, antibodies have binding domains (which are found on the antibody) and these

binding domains interact with specific sites on antigens.

This interaction is analogous to the binding of a virion adsorption protein to the receptor
molecule found on a host cell.
Antibodies are produced in high numbers and in great variety. Generally they are able to
bind to antigens in numerous ways and also to many different parts of antigens.
High specificity of antibody binding:
Individually, antibodies tend to be limited to very binding to very specific regions of
specific antigens.
There exist mechanisms which lead to the evolution, over short periods (days), of
antibody variants which display high specificity as well as strong binding to specific
antigens.
Simultaneously, the production of antibodies which can bind to host proteins is actively
suppressed.
Antibody binding consequently tags an antigen as foreign.
Epitope [antigenic determinant]

Antibody binding site:

An epitope is the specific site on an antigen to which an antibody binds.
Epitopes generally are significantly smaller than the antigens which contain them (and
much smaller than the size of an antibody).
A single antigen often contains numerous epitopes.
Many antibodies to single antigen:
A humoral immune response very often consists of numerous antibodies which
collectively recognize many but not all the epitopes found on a given antigen.
Very often individual epitopes may be recognized by more than one kind of antibody.
Active immunity

Learned immunity:
A normal functioning immune system is capable of recognizing antigens and amplifying
antigen-recognizing cells.
The ability of an animal to recognize and respond to an antigen consequently increases
with exposure (at least to certain limits).
For humoral immunity, the cells which are amplified (increased in number/stimulated to
divide) are those which produce antibody, B cells.
Active immunity simply is this normal "recognize-respond" action of the immune system.
 Passive immunity
Transfer of active immunity:
In contrast to active immunity, passive immunity is the transfer of active immunity from
one individual to another.
Because antibodies are soluble proteins found in the blood, this transferance is relatively
simple and requires, for example, only a simple transfusion of the antibody component of
blood (often called gamma globulin).
Mother to child:
The most important natural occurrence of passive immunity is that from mother to infant.
This occurs either via transplacental transfer or via breast milk, especially colostrum.
Powerful but temporary:
Passively acquired immunity can be very powerful in fighting disease.
The effects of passive immunity, however, are both temporary and cannot be restored
without additional passive infusion.
Passive immunity lasts only as long as infused antibody lasts, which is only on the order
of weeks.
Medically, antitoxin and antiserum play important roles in disease fighting via
administration of passive immunity.
Antiserum [gamma globulin]
Liquid portion of blood:
Serum is the yellow liquid left over following the clotting of blood.
Serum is packed with antibodies.
Serum specificity:
Serum from individuals who have been exposed to a pathogen (or vaccine) usually
contains antibodies that recognize the pathogen (thus accounting for some fraction of the
active immunity displayed by that individual against the pathogen).
Such serum, when employed in passive immunity, is referred to as antiserum.
Antiserum used for passive immunity is often derived from humans or horses though
each source has its problems:
the former is a human blood product and therefore human-derived antiserum potentially
carries human pathogens (though these may be removed by employing various
procedures)
the latter (horse serum) is recognized as foreign by the (human) recipient consequently
making horse-derived passive immunity a treatment which may be safely employed only
once or only a few times before active immunity against horse antigens develop
Artificially acquired immunity
Various medical procedures can induce immunity artifically.
The administration of antiserum is an example of artificially acquired passive immunity.
Vaccinaition, on the other hand, is an example of artificially acquired active immunity.
 Antibody diversity
The ability of an animal to recognize an antigen by antibody-binding is a two-fold
process:
antibodies that bind to the antigen must exist
antibodies that bind to the antigen must exist in sufficient number for recognition to be
acted upon meaningfully
generating variation:
The first criteria is achieved in the course of the replication of antibody-producing cells
(B cells) through a combination of recombination between the genes associated with
many antibody types, and later through the random mutation of antibody genes (the latter
called somatic point mutation).
Amplification of recognizing antibody:
The second criteria is achieved through the amplification of those antibody-producing
cells that produce antibodies which bind novel (not self) antigens.
Humoral immunity, thus, is not so much "acquired" as amplified and refined in response
to exposure to non-self antigens.

Memory:
Once this amplification has occurred it is institutionalized in so-called memory cells.
The existence of memory cells is the physiological manifestation of the priming of
humoral immunity, i.e., for future recognition of specific antigens.
Consequence of antibody binding
Once an antigen is bound by an antibody, any of four actions may occur:
the antigen may no longer function properly (see virus inactivation by antibody)
the antigen and/or attached microorganism may clump (a process called agglutination) or
even precipitate out of solution
complement may be activated
antibody-dependent cell-mediated cytotoxicity may occur if the antigen is found on the
surface of one of the body's own cells

Agglutination:
Agglutination can occur because antibodies display multivalence: An ability to bind more
than one epitope simultaneously (i.e., most antibodies have more than one antigen
binding site).
A consequence of agglutination is increased susceptibility to phagocytosis.
Monoclonal antibodies [Mabs]
Single type of antibody:
Monoclonal antibodies (MAbs) are a way of isolating and making large quantities of only
a single type of antibody.
Remember that though a full complement of antibodies may show great variation in
specificity, individual antibodies tend to be fairly specific in what they will bind and how
strongly they will bind.
Normally pure, large quantities of any individual antibody are difficult to produce within
an animals.
Given the existence of large numbers of pure antibody, however, there exist numerous
techniques one can employ these antibodies in. Particular, these techniques have in
common a requirement for very specific antibody binding.
The primary advantage of monoclonal antibodies (i.e., they come from a single B cell
clone) is that their properties are uniform (within type) and they bind to only a single
epitope. Thus, they have high specificity and predictability.
A downside of MAbs are that their biological properties are very limited compared with
antiserum (polyclonal antibodies) and therefore their ability to recognize different
varieties of individual antigens is limited.
Example: diagnostics:
MAb-based diagnostic tests measure the ability of specific MAbs to bind to specific
antigens, the presence of which might indicate the existence of a pathology such a
pathogen infection.
Other uses of monoclonal antibodies range from numerous applications in basic research
to, potentially, treatment of disease via passive immunization.

Creating MAbs:
MAbs are created by inducing a humoral immune response in an animal (usually a
mouse) then collecting the mouse's B cells (usally they are isolated from the animals
spleen).
These B cells are fused with mouse myeloma (cancer) cells to make them immortal
(otherwise they would eventually die out during propagation in tissue culture). The
resulting cell is called a hybridoma.
The antibody produced by individual hybridomas is characterized.
Desirable hybridomas (i.e., those making antibodies with desirable properties) may be
grown and antibody produced via standard tissue culture techniques.
 Incompatibility across species:
A problem with using mouse monoclonal antibodies in situ (i.e., within patients for
therapeutic reasons) is the same as that experienced when employing horse antiserum,
i.e., recognition by the host as foreign and formation of a host directed humoral immune
response against infused antibody.
These problems may be eliminated, however, by making mouse monoclonal antibodies
more human-like through bioengineering.
Additionally, it is now possible to make human monoclonal antibodies from human B
cells.
Distinguishing self from nonself
How does the body pull off the seemingly miraculous feat of producing a huge variety
(and number) of antibodies seemingly capable of recognizing nearly any antigen the body
is exposed to, but simultaneously not produce antibodies which recognized (bind to) host
cells? For T cell-mediated -immunity, the answer is that T cells mature in the thymus
(hence the name T cell) where they are exposed to all the body's potential antigens and
those which are capable of binding to self are induced to die. B cells, however, are not
matured in the thymus. How is it that B cells which would otherwise bind to self antigens
are rare?
"For nearly 50 years, immunologists have thought that during embryonic development or
early life the immune system undergoes a critical education in which it learns how to
tolerate the body's own tissues while retaining the ability to mount an attack on bacteria,
viruses, and any other foreign invaders." (p. 1665, Pennisi, 1996). However, this dogma,
that the steps involved in distinguishing self from nonself only early in life, turns out to
be not necessarily correct.
Instead, the answer, based on recent research (see Pennisi, 1996), may be that antigens to
which the immune system is exposed simply in very large amounts do not stimulate an
immune response. However, antigens to which the body is exposed in moderate amounts,
especially in a context which the body recognizes as having the hallmarks of infection
("danger!"), do stimulate active immunity. Thus, host antigens, which are highly
prevalent and usually healthy, must suppress the propagation of an immune response
against themselves.
This model may in part explain why it is that infants are less capable of mounting
immune responses especially, for example, against such things as vaccines. These very
small people may perceive the antigen found in a normal vaccination to be so large
(relative to themselves or, actually, the number of their "T cells and antigen-presenting
cells" p. 1666, Pennisi, 1996) that it is perceived as "self." Later in life, when these small
people are no longer quite so small, the ratio of antigen to body size (i.e., "T cells and
antigen-presenting cells") is sufficiently larger that the antigen is not recognized as "self"
and consequently can induce a reasonable immune response.
In addition, "If reasearchers can control the type of immune response they induce by
adjusting how much antigen they give relative to the amount of T cells and antigen-
presenting cells in the recipients, they might, for example, be able to make people
undergoing organ transplants tolerant to the donor tissue or arrest autoimmune diseases."
(p. 1666, Pennisi, 1996)