The importance of genetic recombination and post recombination events related to diversity in antibodies Concept introduction: Antibodies are the potential receptors that can recognize unique aspects of antigen present on the pathogen. Antibodies are produced by the differentiation of B cells into plasma cells. Based on the physical, chemical, and immunological properties, antibodies are classified into 5 classes namely IgG, IgA, IgM, IgE, and IgA. All the antibodies share a common structural similarity by having 2 light and 2 heavy chains. Each light and heavy chain are further classified into “constant (C) and variable (V) domains”. Disulphide bonds connect one light chain with another heavy chain. Each heavy and light chain is derived from the combination of several gene fragments generated after several events of recombination.

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Chapter 27, Problem 2AQ

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The importance of genetic recombination and post recombination events related to diversity in antibodies

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Antibodies are the potential receptors that can recognize unique aspects of antigen present on the pathogen. Antibodies are produced by the differentiation of B cells into plasma cells. Based on the physical, chemical, and immunological properties, antibodies are classified into 5 classes namely IgG, IgA, IgM, IgE, and IgA. All the antibodies share a common structural similarity by having 2 light and 2 heavy chains. Each light and heavy chain are further classified into “constant (C) and variable (V) domains”. Disulphide bonds connect one light chain with another heavy chain. Each heavy and light chain is derived from the combination of several gene fragments generated after several events of recombination.

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Most of the enzymes involved in immunoglobulin gene rearrangement are ubiquitously expressed in all cells of the body. However, the specific recombination events between V, J, and D gene segments that generate antibody diversity occur only in developing B cells. How do RAG-1 and RAG-2 ensure that recombination takes place at antibody gene segments?

In rare instances, B cells can be found that have two immunoglobulin light chain alleles, both of which are rearranged in frame, and can encode functional light chain proteins. Yet, on the surface of the B cell, only one of the two light chain proteins is detected in the membrane-bound immunoglobulin receptor. The reason these rare cells have two functional light chain rearrangements but only express one of the two light chains as part of the B-cell receptor is: One of the two light chains is formed from rearrangement of a V gene segment that is a pseudogene. One of the two light chain proteins doesn’t form a stable complex with the heavy chain expressed in this cell. One of the two light chain alleles is not transcribed efficiently, and produces only low levels of protein. One of the two light chain alleles uses a V gene segment that is not targeted very often by the RAG recombinase. One of the two light chains is rapidly degraded after synthesis due to improper folding.

Suppose that a particular species of vertebrate animal has immunoglobulin heavy-chain genes that include 55 V segments, 21 D segments, and 8 J segments, and has immunoglobulin light-chain genes that include 41 V segments and 6 J segments. How many different immunoglobulin structures could be produced by mature B-lymphocytes? (Assume that segments are spliced without any junctional variation or imprecision).