In the last video, we discussed that antigens are small “identificators” on pathogens which bind to antibodies at the epitope on the antigen and the paratope on the antibody. Antibodies, also known as immunoglobulins, are in turn secreted by B cells to neutralize pathogens. In a word, they act as a “first line” of defence for the body’s immune system. They can do this by on one end, connecting to the invading pathogen through its antigen and on the other end, connecting to various white blood cells.
This here is a single antibody, called a monomer, but antibodies consisting of multiple individual antibodies also exist, such as a pentamer, shortened as IgM, and a dimer, shortened as IgA.
Let us zoom in on the structure of an antibody. In general, antibodies are Y shaped molecules and contain a variable region, shortened as the Fab region, in addition to a constant region, shortened as the Fc region. The variable or Fab region binds to molecules. The constant or Fc region on the other hand determines what isotope, or class, the antibody in question belongs too.
There are 5 classes of antibodies; IgM, IgG, IgD, IgE, and IgA. However, we will only examine IgM and IgG closer in this video:
1. IgM (μ) is the first antibody produced and expressed following exposure to an infectious agent. Its main task is to aid the immune response through agglutination, in other words forming clots of antibody-pathogen aggregates. Put even more simply it sticks to the pathogen and to other antibodies, thereby slowing it down.
2. IgG (γ) main antibody found in the blood and is responsible for opsonization, that is to say assisting phagocytosis or put even more simply it helps the phagocyte to eat the bacteria. In addition it also aids the immune response through agglutination.
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