How are antibodies produced?
Antibodies are produced by:
Antibodies are produced by,Our bodies have a dedicated army to search and destroy, and antibodies play a major role in this battle.
Antibodies are specialized Y-shaped proteins that bind to foreign bodies that enter the body – such as viruses, germs, fungi, and parasites – with a mechanism similar to a lock and key.
Antibodies (Search Brigade) in the Search and Destruction Army of the immune system, whose mission is to find and distinguish hostile bodies with the aim of destroying them.
“The antibodies are released from the cell and the search begins,” says Dr. Warner Green, director of the HIV Treatment Research Center at the Gladstone Foundation in San Francisco.
When the antibodies find their target, they bind to it, triggering a chain reaction that kills the intruder. Antibodies are part of what is called the immune system, as it learns to recognize and remove specific pathogens.
What do antibodies look like?
The two upper arms of the Y-like antibody bind to what is known as the antigen, which may be a molecule or a piece of molecule, and is often part of the germ or virus. For example, the new Corona virus has unique spines on its outer shell, and some antibodies bind to the proteins of these spines and recognize them.
The lower or leg section of the antibody binds to some other parts of the immune system. These parts can kill the antigen or stimulate the immune system in other ways, including by stimulating complementary protein chain reactions.
“The proteins are really the ones that work,” says Dr. Green, as they form holes in the target cell, such as the envelope of the virus.
“All antibodies – also called immunoglobulins (Ig) – have the same basic shape, but they are divided into 5 different types, namely IgG, IgM, IgA, IgD and IgE,” said Dr. Jason Sester, a professor of immunology and microbiology.
Each of these types is slightly different in shape and plays a different role in the immune system. For example, IgG is a single piece similar to the letter Y, and IgM is made of 5 compact segments, each of which binds to a different antigen.
IgG and IgM antibodies spread into the bloodstream and enter the organs, while IgA antibodies are excreted from the body along with mucus and secretions, while IgE antibodies usually trigger allergic reactions, such as allergic to peanuts or pollen.
The IgD antagonist has long been obscured, but it plays a role in activating the cells that produce the antibodies.
Where do antibodies form?
“You need to know B cells to understand antibodies,” said Dr. Simon Goodman, director of technical programs at the Antibody Society Foundation, a non-profit that represents those working in antibody research and development. “These cells are white blood cells that form in the bone marrow. There are about a trillion B cells in the body, each with a unique IgM antibody on its surface, and each of them binds to a different antigen.”
This tremendous variety allows the body to recognize almost any substance it might get into. This diversity results from the mixing of genes responsible for the binding site of each antibody – such as shuffling of playing cards – in each B cell. “The scale of the rearrangement that is taking place is enormous,” says Dr. Sester.
These B cells roam the body, remain elongated in places such as lymph nodes and tonsils, and remain unattached most of the time. But if a B cell binds to an antigen – a possibility of one in a million – it stimulates the other B cells. It increases in size by a process known as clonal expansion.
The resulting cells are identical to the parent cells, and after about a week hundreds of thousands to millions of these copies form. Ultimately, these expanding B cells clonally differentiate into plasma cells, which are factories of antibodies, as they secrete 10,000 antibodies from each cell per second, and this process continues for weeks or years, sometimes.
Goodman says: “If we count the B cells as locks, we can count the bodies that rotate in the body as keys, some of which may fit the lock well and some of them are less compatible, and some of them may not be compatible at all, and depending on this compatibility between the fine particles and the lock on the surface of the B cell.
The cell interacts and divides. ”As B cells multiply, they produce more plasma cells, and they produce specific antibodies.
The body does not produce one type of antibody, but rather an enormous number of them, each of which binds to a different part of the foreign particle.
Dr. Green says:
“Not all antibodies do the same thing when they bind to the intruder. Some stop the infection and nullify the threat directly by preventing the particle from entering the cell, and others mark the particle for the killer cells – which are not antibodies – in the immune system to recognize and remove it.
Some surround the virus or bacterium, forming a sticky coating, and some tell immune cells called phagocytes the presence of the particle to swallow.
This process may produce adverse results with viruses that may adapt to this mechanism to invade other cells.
“The first type of antibody to form upon exposure to a virus is IgM, which appears in the body 7-10 days after exposure to the virus and is associated with it.
The binding of the five pieces of the antibody to the antigen is weak if they are each separately, but they are bound together forming a strong bond. ”
After 10-14 days, the body begins to form the antibody IgG, which is the main laboratory for the immune system, and it can pass through the placenta to give the fetus negative immunity against some diseases until its immune system is complete.
The immune system is usually very accurate in recognizing enemies and ignoring the body’s own cells, but this process may sometimes fail, when the T cells, which are another type of white blood cells, intervene, as the body uses them to double-check targets, so the immune response occurs only when you know Both B and T cells appear on the particle as a foreign body.
The body is supposed to eliminate B cells that produce autoantibodies that interact with the body’s own cells, but if this does not happen, the body may target and destroy its own cells, which causes autoimmune diseases, such as lupus, rheumatoid arthritis, and type 1 diabetes.
There are more than 100 autoimmune diseases according to the American Autoimmune-Related Diseases Foundation.
What are monoclonal antibodies?
“Antibodies have become the basis for many useful drugs, in addition to some of the most powerful laboratory technologies in biology, the most important of which is the so-called monoclonal antibodies,” says Dr. Goodman.
Researchers inoculate animals – or humans – to stimulate the production of antibodies specific to a specific substance.
The body gradually makes more effective antibodies to the antigen. These antibody-producing cells are purified from leukocytes and placed in dishes to see which one binds best to the antigen, then the most powerful cells are isolated, forming factories dedicated to the super-selective antibody.
This cell fuses with a cancer cell, forming what is called a hybrid or monoclonal neoplastic cell, and this hybrid cell is a permanent manufacturer of the same antibodies over and over again.
The monoclonal cell fuses with a cancer cell because it does not stop reproducing, and these cells continue to produce antibodies without stopping.
They are amazingly accurate tools, each cell line has many uses, and there are millions of commercial antibodies that are used in the laboratory to distinguish the smallest and most accurate cellular targets.
Antibodies form the basis of many of the best-selling drugs:
For example, adalimumab (Humira) is a monoclonal antibody used in the treatment of rheumatoid arthritis by inhibiting inflammatory proteins known as cytokines, and bevacizumab (Avastin) targets a molecule that fuels blood vessel growth, which by targeting it can inhibit The growth of some types of cancer such as lung, colon, kidney and brain cancer.
Dr. Green says:
“Doctors around the world are racing to produce monoclonal antibodies that can stop the new Corona virus. These antibodies are purified from the plasma of patients who have recovered from Covid-19 disease, as we hope to find the most effective antibodies and produce them in large quantities, and thus doctors can create temporary negative immunity until the body forms an appropriate long-term immune response. ”
Polyclonal antibodies are produced from multiple B cells and are a library of antibodies that bind to different parts of an antigen or target. It is usually produced by injecting an animal with an antigen, stimulating an immune response. Then the animal’s plasma is extracted to produce the antibody in large quantities.
Whereas monoclonal antibodies may take 6 months, it takes 4-8 weeks to produce polyclonal antibodies, and requires less technical expertise, in addition to providing greater chances of detecting a specific antigen in certain tests, which makes it more sensitive. Equally large amounts of them, as each animal produces a different pattern.
How are the antibody tests performed?
These tests reveal has the body produced significant amounts of antibodies specific to a specific molecule? This reveals that the person was exposed to a virus or germ infection in the past. These tests usually detect IgG and IgM antibodies.
Tests for emerging corona virus:
Tests for the emerging corona virus reveal part or all of the proteins of the superficial spines of the virus, thus revealing has the person been infected with the virus?
The tests give positive results two weeks after the first exposure to the pathogen, because it takes time for the body to increase production of the antibodies.
There are two common types of antibody detection tests:
the side-flow test and the enzyme-linked immunoassay (ELISA) test. Both involve fixing an antigen to a surface and detecting any antibody binding to it.
Typically, a chemical reaction such as fluorescence or color change occurs when the antibody begins to bind to the antigen. In essence, a lateral flow test is similar to a home pregnancy test in that blood or serum is applied to a surface, usually paper.
The ELISA test :
The ELISA test works on a similar principle, with the difference that the test is performed on thin sheets and requires a laboratory technician, and the results are not read directly.
Good tests produce little false positive or negative results, and to ensure this happens, scientists must calibrate their tools, such as ensuring that samples that do not contain antigen give false positive results, that is, testing blood samples taken before the spread of the Corona pandemic, for example, and verifying that none of them give positive results.
Samples containing antibodies must be definitely tested to ensure the test can detect them.
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