An antibody is a class of proteins called immunoglobulins, which are made by specialized white blood cells to identify and neutralize materials foreign to the immune system.
Shaped like a ‘Y’, antibodies have a highly-variable region in their thorns, which allows the immune system to tailor its response to an untold range of threats.
This unique makeup of various antibodies allows them to bind specifically to complex chemical signatures, known as antigens, on the outer layers of invasive pathogens such as viruses and bacteria, as well as cancer cells. are found.
By binding with these surface markers, antibodies can interfere with the functions of the cell or microbe, providing them with immanol or unable to carry out the functions required for replication.
Their binding can also trigger two types of immune responses.
The body contains a domino-effect between changes in the form of complementary systems of signaling molecules. This cascade of chemical reactions can have a range of effects on the body, inhibiting many immune responses, such as inflammation as well as physically disrupting and destroying the pathogen.
A second reaction, called opsonization, recruits specialized white blood cells called phagocytes to ingest and perhaps even digest the target material.
What makes antibodies so specific?
Antibodies are produced inside white blood cells known simply as B-cells. These cells begin life inside the bone marrow, before they mature they circulate through the body’s blood vessels.
Part of their development involves assembling key segments of the immunoglobulin gene to churn antibodies with random structures. Thanks to the mix and match genetics of antibody production, humans can produce unique antibodies up to one quintal.
B-cells that produce antibodies that match the material found inside their body before being made into the bloodstream. Exceptions give rise to a class of disorders known as autoimmune disease.
Antibodies from mature B-cells that successfully bind foreign antigens are encouraged to reproduce, swelling their numbers to provide a multitude of antibody ‘factories’ that can deal with a potential infection. .
Some B-cells can be preserved in the body for years, creating a list of past infections that can quickly deploy in the event of future infections.
How are antibodies used in medicine?
Antibodies can be used both directly and indirectly as treatments for disease, as a preventive form of therapy and in diagnosis.
Vaccines provoke B-cells to maintain and preserve the supply of antibodies by introducing antigens, in hopes of future infection.
Alternatively, specific infection (or monoclonal) antibodies can be generated outside the body for treatment against existing infections or diseases, targeting cancer cells or even animal toxin.
Monoclonal antibodies can also be applied to laboratory samples to detect the presence of antigens in test substances. A common pathology test, called an enzyme-linked immunosorbent assay (ELISA), for example, uses colored dyes to indicate the presence of an antigen sticking to antibodies attached to diagnostic kits.