The use of two polyclonal activators, dextran sulfate (DxS) and lipopolysaccharide (LPS), with or without the presence of additional antigen, is presented here as a system for exploring the antibody response of normal (naive) and primed B cells. This system expands populations of cells not normally observed under in vivo regulation. By fusing such unnaturally activated B cells, anti-p-azophenylarsonate hybrids were produced that secrete different isotypes of antibodies. The frequencies of isotopes expressed by these hybrids may correspond to the chromosomal order of the heavy chain genes because greater numbers of IgM- and IgG3-secreting hybrids were produced than IgG(2a) hybrids. Only one IgA hybrid was observed. When DxS and LPS were used to stimulate antigen-primed B cells, hybrids were generated that simultaneously secrete two isotopes of antibody. These hybrids may represent a model of the antigen-stimulated maturational class-switch step observed in normal B cells that involves the expression of IgM and IgG isotypes by the same cell. Such hybrids offer an opportunity to study antibody regulation and diversity by examining the rearrangement of genes during the Ig switch, by exploring the nature of the necessary transitions of mRNA transcription and translation to produce functional antibodies, and by probing the structure and specificity of such antibodies.
|Original language||English (US)|
|Number of pages||5|
|State||Published - 1982|
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