Question

1. Do some research and explain how an antibody can be produced that reacts with another antibody

Answer 1

An antibody is a secreted form of a receptor that occurs on the surfaces of B cells. Each B cell clone makes IgM with different binding characteristics—that is, the variable binding regions of the IgMs differ. The host has a large repertoire of naive B cells that produce a diverse array of IgM specificities.

An antigen on first exposure to a host will often bind rather weakly to several of the naive IgM. Those B cell clones with relatively high-affinity IgM for the antigen divide rapidly and come to dominate the antibody response to the antigen.

The dividing B cell clones undergo affinity maturation for particular epitopes. During this process, elevated mutation rates occur in the DNA that encodes the antibody binding region. This hypermutation in dividing B cell lineages creates a diversity of binding affinities. Those B cells with relatively higher binding affinities are stimulated to divide more rapidly than B cells with lower affinities. This process of mutation and selection creates high-affinity antibodies for the antigen.

The B cells that win the competition and produce affinity matured antibodies switch from producing IgM to immunoglobulin G (IgG). This class switch occurs by a change in the nonvariable region of the antibody that is distinct from the variable binding region.

The matured antibody had an affinity for the epitope 30,000 times higher than the original, naive antibody. This increased affinity resulted from nine amino acid substitutions during affinity maturation. The naive antibody significantly changed its shape during binding with the epitope. By contrast, the mature antibody had a well-defined binding region that provided a lock-and-key fit to the epitope. speculated that naive antibodies may have more flexible binding regions in order to recognize a wide diversity of antigens, whereas matured antibodies may develop relatively rigid and highly specific binding sites.

Naive IgM may bind a broader array of antigens at lower affinity, whereas matured IgG may bind a narrower array of antigens at higher affinity. Most analyses of epitope binding focus on IgG antibodies that have been refined by affinity maturation. Recently, attention has turned to the binding characteristics and different types within the IgM class, including the natural antibodies.

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