Immunity produces Antibodies, which are Protective Proteins

 

Antibodies 

Antibodies are proteins that protect you when you are exposed to a foreign material. Antibodies are proteins produced by your immune system that attach to undesirable substances and remove them from your body. Immunoglobulin is another term for antibody. Antibodies, also known as immunoglobulins, are glycoproteins that are created in the body in reaction to invading foreign particles (antigens) such as bacteria and viruses. As a result, they're important in the immune system's fight against infection and illness.

Antigens can be proteins, such as cancer cell receptors, sugars on bacterial and viral cell surfaces, hormones, chemical substances, or nucleic acid structures that Antibodies identify and bind. The epitope is the part of an antigen that interacts with an antibody. Normally, an animal's immune system will produce a huge number of antibodies that identify several antigen epitopes. Each antibody may be specific for a particular epitope and is released by a separate antibody-producing plasma cell. Polyclonal antibodies are those present in serum that are generated by a large number of plasma cells (clones). While this is a benefit for battling diseases in nature, polyclonal antibodies' variability restricts their use as research tools.

The invention of a technology for manufacturing monoclonal antibodies by Köhler and Milstein in 1975 was a key milestone in the production of antibodies for scientific purposes. The procedure includes extracting B cells (plasma cell progenitors) from the spleen of an antigen-challenged animal and fusing them with an immortal myeloma tumour cell line. A hybridoma is a single-cell hybrid that develops from this process. The B cells allow hybridomas to produce antibodies, while the myeloma cells allow them to proliferate endlessly and thrive well in vitro. Hybridomas produce just one kind of antibody, thereby providing a long-term supply of monoclonal antibodies that are selective for a particular epitope.

Structure of Antibodies-

Because IgG is the most common antibody in serum, many of the fundamental structural properties of antibodies may be highlighted using it as a model. An antibody is traditionally shown as a Y-shaped molecule made up of four polypeptide subunits with two identical heavy and light chains.

Each heavy chain's N-terminus joins with one of the light chains to form two antigen-binding domains. Fragment antigen binding (Fab) domains are what make up the "Y" shape's arms. The fragment crystallisation (Fc) domain, which represents the tail of the "Y," is formed when the C-termini of the two heavy chains join. The Fc domain is important for the antibody’s interaction with effector cells such as macrophages and for activation of the complement cascade. The four polypeptide chains are held together by covalent disulfide bridges and non-covalent bonds.

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