History, Development And Effectuation Of Monoclonal Antibody Sequencing

In response to foreign proteins, which are called antigens

, the B lymphocytes of the immune system produce special proteins called as antibodies. Antibodies function as markers, binding to the antigen so that the antigen molecules can be recognized and destroyed by phagocytes. Antibody binds to a part of the antigen called the epitope. Therefrom, the epitope is short amino acid sequence, which the antibody is able to recognize. The availability of amino acid sequences of antibody proteins established the fact that the body can and does produce many different antibody proteins with similar antibody constant regions and divergent antibody variable regions. The team comprising Edelman and his colleagues used cyanogen bromide and proteases to fragment the antibody protein subunits into smaller pieces that could be analyzed for determination of their amino acid sequence. In 1969, the first complete antibody sequence, which was determined, was the largest complete protein sequence that had ever been determined.

Structurally, antibodies are proteins comprising four polypeptide chains. These four chains form a quaternary structure resembling a Y shape to a certain degree. In an organism, each B cell synthesizes only one kind of antibody. However, in an organism, an entire population of different types of B cells exists. Respective antibodies too these B Cells were produced in response to the various antigens, which the organism had been exposed to. However, to be considered useful as a tool, molecular biologists require significant amounts of a single antibody (and that antibody exclusively). Therefore, to culture a population of B cells derived from a single ancestral B cell, such that this population of B cells allows us to harvest a single kind of antibody a method has been developed. This cultured population of cells would, thus, be correctly described as monoclonal, and the antibodies so produced by this population of B cells are called, Monoclonal Antibodies. In contrast, antibodies obtained from the blood of an immunized animal are called polyclonal antibodies. In 1975, Georges Kohler and Cesar Milstein pioneered the production of monoclonal antibodies.

In Monoclonal Antibodies, two features of the antibody-epitope relationship are key essential as molecular tools. Specificity and Sufficiency.

1. Specificity the antibody binds only to its particular epitope

2. Sufficiency the epitope can bind to the antibody on its own, i.e. the presence of the whole antigen molecule is not necessary

Monoclonal Antibodies are required in various academic, medical and commercial applications, especially clinical research. Several diagnostic tests used for determining small amounts of drugs, toxins or hormones, e.g. monoclonal antibodies to human chorionic gonadotropin (HCG) are used in pregnancy test kits require the presence of antibodies. Another more known diagnostic, which uses antibodies, is the diagnosis of AIDS by the ELISA test. Monoclonal Antibodies are also extensively used in the radioimmunodetection and radioimmunotherapy of cancer amongst which, certain new methods can even target only the cell membranes of cancerous cells. In November 1997, the FDA approved Ritoxin, a new cancer drug based on monoclonal antibody technology. The problem of organ rejection in patients, who have had organ transplants, has seen successful treatments developed using Monoclonal Antibodies called as OKT3, which is an antibody to the T3 antigen produced by T cells of the human immune mechanism. A strain of single pathogen such as Neisseria gonorrhoeae have been successfully classified using Monoclonal Antibodies Sequencing. Quite a few traditionally considered "untreatable" viral diseases have found solutions developed using Monoclonal Antibodies Sequencing. At the pace at which current clinical research is leaping ahead, several research specialists hold the opinion that antibody sequencing could be an important tool in the race to defeat the HIV virus, and cure AIDS.

by: Paul Kerr

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