Knowles D P, Perryman L E, McElwain T F, Kappmeyer L S, Stiller D, Palmer G H, Visser E S, Hennager S G, Davis W C, McGuire T C
Animal Disease Research Unit, US Department of Agriculture, Pullman, WA 99164-7030, USA.
Vet Parasitol. 1995 Mar;57(1-3):93-6. doi: 10.1016/0304-4017(94)03113-b.
The competitive inhibition ELISA (CI-ELISA) format overcomes problems associated with antigen purity since the specificity of the CI-ELISA depends solely on the monoclonal antibody (mAb) used. Therefore, the CI-ELISA format is well suited for use with recombinant antigens. Molecular clones expressing a conserved 19 kDa protein of Anaplasma marginale and a 34 kDa protein of Babesia equi were derived and characterized. The 19 kDa A. marginale protein, conserved in all recognized Anaplasma species, and present in the infected tick salivary gland, was reactive with all bovine immune sera tested. The 34 kDa B. equi protein contains a protein epitope bound by antibody in equine immune sera from 19 countries. Monoclonal antibodies reactive with these proteins were derived and applied with recombinant copies of the 19 kDa A. marginale and 34 kDa B. equi proteins in a CI-ELISA format.
竞争性抑制酶联免疫吸附测定(CI-ELISA)方法克服了与抗原纯度相关的问题,因为CI-ELISA的特异性仅取决于所使用的单克隆抗体(mAb)。因此,CI-ELISA方法非常适合用于重组抗原。表达边缘无形体保守的19 kDa蛋白和马巴贝斯虫34 kDa蛋白的分子克隆已获得并进行了表征。在所有已识别的无形体物种中保守且存在于受感染蜱唾液腺中的19 kDa边缘无形体蛋白,与所有测试的牛免疫血清均有反应。34 kDa马巴贝斯虫蛋白包含一个蛋白表位,来自19个国家的马免疫血清中的抗体可与之结合。获得了与这些蛋白反应的单克隆抗体,并将其与19 kDa边缘无形体和34 kDa马巴贝斯虫蛋白的重组拷贝一起应用于CI-ELISA方法中。