Antibodies, Antigens, and Antioxidants

  • Antibodies, Antigens, and Antioxidants
  • "Antibodies, Antigens, and Antioxidants"

What are Antibodies?

There are many things that people hear about when they are looking up information on health regarding antibodies. In many cases, they don't know what antibodies are. Antibodies are proteins that are shaped like Y's. They are mainly produced by plasma cells. The immune system uses these agents in order to find pathogens like bad bacteria and certain virus and neutralize them. Among the things that they recognize in the harmful agent is an antigen. Antibodies are different from Antioxidants.


types of antibodies
The antibody contains tips that carry a paratope for a specific epitope of the antigen. This is similar to a lock for the key. The antibody locks on to the antigen precisely. The antibody has a binding mechanism that it can use in order to find an infected cell or microbe. Another thing that the antibody could do is tag the target so that other parts of the immune system could take care of the infection or microbe. Among the things that the antigen could do is block a certain part of the microbe which makes it possible for it to survive and invade different parts of the body. This allows an impediment of the biological process of the disease and even recruit the assistance of macrophages to take care of the problem.

What do Antibodies do?

One very fascinating aspect of the antibody is its ability to communicate with the other members of the immune system. The antibody has an Fc region that allows it to send messages to other members of the immune system. The Fc region has a glycosylation site which handles the interaction between the antibody and the other components. The humoral immune system is what creates the antibodies. The antibody is one of the highly advanced forms of bodily defense mechanisms that are used for defending the body.

Where are antibodies created?

Antibodies are created by the humoral immune system and then released by B cells. Typically, the type of B cells that do the job of releasing the antibodies are plasma cells. There are two typical forms of antibodies. One is a form that is soluble and can be released into the blood plasma. Then there is the form that is connected to the B cell at the surface and is used as a receptor by the B cell. The receptor deals with the activation of the cells. They are eventually differentiated into plasma cells or memory B cells. Memory B cells are good for keeping the antigen in memory. When the B cells can remember the antigen, they can respond faster in the case that it finds the antigen again.


There are many cases where the B cell is partnered up with a T helper cell so that the activation of the B cell could be complete. This allows for the antibody to be generated. There will be more antibodies to bind with the antigen as a result. The blood and tissue are often filled with antigens so that the areas could be checked for antigens or other microorganisms that are invading.


Antibodies belong to the immunoglobulin superfamily. They make up the majority of the blood proteins from the gamma globulin portion. They come in many different isotypes and structures. Among the fascinating things to look at is the interaction with the antigens. This is achieved by the paratope of the antibody as it interacts with the epitope of the antigen. The interaction of an antibody with an antigen is done in the lock and key style. Often times, there is a weak and general interaction with the hydrogen bonds, electrostatic forces and other aspects of the antibody and antigen interactions. This often becomes an immune complex when the antibody and antigen comes together.

Antibodies Structure

The structure of the antibody is one very interesting aspect to look at. For one thing, they have chains of sugar that accompanies the residues of amino acid that have been conserved. They are a proteins with attached glycans. The antibodies need the glycas in order to maintain structure and functionality. It also has immunoglobulin domains, or Ig domains which is made of polypeptide chains. These chains are basically two light chains that are connected with the use of disulfide bonds. There are also heavy chains that make up the antibodies.


The heavy chains come in five types that are named by different Greek letters. This also gives an indication of the antibody's class. The chains vary from each other in size as well as how they are structured. One thing that every heavy chain has in common is that they have two regions. One region is constant while the other region is variable. One contributing factor to the differences between each heavy chain is the different B cells that produce the heavy chain. The chain has the length of around 110 amino acids. This is a lot different from the light chain which has up to 217 amino acids in length.

Antibody functions

There are variable functions of the antibody that depends on the regions and the parts of the antibody. For instance, the antibody has arms that can connect to antigens. This region is called the fragment antigen-binding region. Both the light and heavy chain antibodies have a paratope at the end of the monomer of the antibody. The variable domains of the antibody chains are what shape the paratope. These are responsible for connecting the antibody to the antigen and taking care of the antigen. Antbody's do have quite a helpful mechanism for maintaining the health of the body and the immune system.


Antibodies are very fascinating in that they help the body maintain its health. With the components that is in use for the finding of the virus or the bacteria that is a threat to the living body, antibodies are very powerful and efficient in getting rid of the problem. The memory aspect of the antibody is also very helpful in the case that the antigen gets away. The antibody will remember the antigen and approach it again and either neutralize it by itself or communicate with the other components of the immune system in order to get rid of the threat.