Activation of mouse B cells with lipopolysaccharide in conjunction with anti-immunoglobulin (Ig) antibodies results in interleukin 2 (IL2) receptor (IL2-R) expression and IL2 responsiveness. In most studies on the effect of IL2 on antibody production by B cells, polyclonally activated normal B cells or B cell lines established in vitro have been used as indicator cells, thus allowing no direct correlation between the experimental findings and the actual physiological mechanism of IL2 action in antigen-specific B cell response. We employed the splenic fragment culture technique, which measures antibody response on the clonal level, to analyze the effect of purified human recombinant IL2 (rIL2) on the primary antigen-specific Ig response of mouse B cells. Here we report that rIL2 increased the frequency of dinitrophenyl (DNP)-responsive splenic B cells and the amount of Ig secreted per clone. The anti-DNP antibody response was dependent upon interaction of naive B cells with carrier-primed T cells, which apparently provided the signal for IL2-R expression. Recombinant IL2 also facilitated Ig isotype switching by individual clones, suggesting a role for IL2 in activation, maturation and differentiation of antigen-specific naive B cells in their response to T-dependent antigens.
|Number of pages||9|
|State||Published - 1 Jan 1989|
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