Scheerlinck J P, DeLeys R, Saman E, Brys L, Geldhof A, De Baetselier P
Institute of Molecular Biology, Vrije Universiteit Brussel, St-Genesius-Rode, Belgium.
Mol Immunol. 1993 Jun;30(8):733-9. doi: 10.1016/0161-5890(93)90144-z.
Immunization of different mice strains with a recombinant fusion protein composed of the vector-encoded N-terminal leader peptide CroLac (containing lambda Cro and LacI fragments) and a part of the transmembrane protein of HIV-1 (gp41) led to a high anti-CroLac humoral immune response. A detailed analysis of this response revealed the presence of an immunodominant, linear B cell epitope localized near the C-terminus of the CroLac fragment. The immune response seemed to be biased towards this epitope since few or no monoclonal antibodies (mAb) could be generated against the remaining part of CroLac and the gp41 fragment. Upon removal of the immunodominant region from the fusion protein the immune response was redirected and spread over the previously non-immunogenic regions. Consequently, we report a model system in which an immunodominant B cell epitope biases the immune response away from less immunogenic epitopes on the same molecule.
用由载体编码的N端前导肽CroLac（包含λ Cro和LacI片段）和HIV-1跨膜蛋白的一部分（gp41）组成的重组融合蛋白对不同小鼠品系进行免疫，引发了强烈的抗CroLac体液免疫反应。对该反应的详细分析显示，存在一个免疫显性的线性B细胞表位，定位于CroLac片段的C端附近。由于针对CroLac其余部分和gp41片段几乎无法产生单克隆抗体（mAb），免疫反应似乎偏向于这个表位。从融合蛋白中去除免疫显性区域后，免疫反应重新定向并扩散到先前无免疫原性的区域。因此，我们报道了一个模型系统，其中免疫显性B细胞表位使免疫反应偏离同一分子上免疫原性较低得表位。
