Theopold U, Köhler G
Max-Planck-Instiut für Immunbiologie, Freiburg, FRG.
Eur J Immunol. 1990 Jun;20(6):1311-6. doi: 10.1002/eji.1830200617.
A transgenic mouse line was produced which allowed the expression of E. coli beta-galactosidase (beta-Gal) under the regulatory elements of the immunoglobulin heavy chain locus. Expression of the transgene is found in spleen and bone marrow. Upon immunization of the transgenic mice with beta-Gal, a reduced but clearly detectable antibody response was obtained. Affinity purification with sera from immunized transgenic mice suggests that they contain lower affinity antibodies as compared to normal littermates. Transgenic and nontransgenic mice immunized with bovine serum albumin (BSA) alone or as a mixture with beta-Gal gave comparable anti-BSA responses. Immunization with a chemically cross-linked (Gal-BSA)-protein, however, showed a 10- to 30-fold difference in the anti-BSA response. Partial unresponsiveness to beta-Gal in the transgenic mice is best explained by a dominant, peripheral suppression mechanism linked to the antigen-presenting potential of B cells.
构建了一种转基因小鼠品系,其可在免疫球蛋白重链基因座的调控元件控制下表达大肠杆菌β-半乳糖苷酶(β-Gal)。在脾脏和骨髓中可检测到转基因的表达。用β-Gal免疫转基因小鼠后,可获得减弱但明显可检测到的抗体反应。用免疫后的转基因小鼠血清进行亲和纯化表明,与正常同窝小鼠相比,它们含有亲和力较低的抗体。单独用牛血清白蛋白(BSA)或与β-Gal混合免疫转基因和非转基因小鼠,产生的抗BSA反应相当。然而,用化学交联的(Gal-BSA)蛋白免疫时,抗BSA反应显示出10至30倍的差异。转基因小鼠对β-Gal的部分无反应性,最好用与B细胞的抗原呈递潜能相关的显性外周抑制机制来解释。