The immune response to an isomaltohexosyl-protein conjugate, a thymus-dependent analogue of alpha(1 replaced by 6) dextran.

Abstract

Two oligosaccharides derived from B512 dextran (Dex), isomaltohexaose (IM6), and isomaltotriose (IM3) have been coupled to keyhole limpet hemocyanin (KLH) and the conjugates studied as thymus-dependent (TD) immunogens analogous in their specificity to Dex. Both IM3-KLH and IM6-KLH stimulate an anti-Dex response in CBA mice. In C57BL mice, only IM6-KLH stimulated an anti-Dex response; IM3-KLH, although immunogenic, failed to elicit the production of anti-Dex antibodies. Similarly, CBA anti-Dex antibodies cross-reacted with both IM3 and IM6 coupled to bovine serum albumin (BSA), whereas C57BL anti-Dex antibodies cross-reacted with IM6-BSA and bound IM3-BSA only very poorly. This reciprocal lack of cross-reactivity between IM3 conjugates and Dex in C57BL mice was controlled by genes linked to the IgH locus, as shown in responses of allotype congenic CBA mice. This genetically regulated fine specificity pattern was overridden when IM6-KLH was used for immunization. C57BL antibodies that bound both Dex and IM3-BSA were produced in response to this antigen. Thus, isomaltohexosyl-protein conjugates provide Dex-like antigens that differ from Dex itself in terms of thymus dependency and the fine specificity of the precursors that are activated. They should provide important tools to study the activation requirements of antigen-specific B cells.