Knapp B, Shaw A, Hundt E, Enders B, Küpper H A
Research Laboratories of Behringwerke AG, Marburg 1, W.-Germany.
Behring Inst Mitt. 1988 Apr(82):349-59.
We have isolated a cDNA clone coding for 165 amino acids of a histidine alanine rich protein. An extended repeat region of this clone codes for the tripeptide Ala-His-His, which is extremely conserved, and for the tripeptide Ala-Ala-Asp, which shows only slight variability among the repeat units. This antigen exhibits high homology to the HRPII antigen described by Wellems and Howard (1986). The coding region was expressed in E. coli as a MS2-polymerase fusion protein, which was purified and used for immunization of Aotus monkeys. The animals immunized with this fusion protein showed only low parasitemias (less than 2%) after infection with P. falciparum, while animals from the control group or animals immunized with a MS2-fusion protein carrying other malaria specific sequences were not protected. The result suggests that this antigen is a good candidate for a malaria vaccine.
我们分离出了一个编码富含组氨酸和丙氨酸蛋白165个氨基酸的cDNA克隆。该克隆的一个延伸重复区域编码三肽Ala-His-His,其高度保守,还编码三肽Ala-Ala-Asp,其在重复单元间仅表现出轻微变异。这种抗原与Wellems和Howard(1986年)描述的HRPII抗原有高度同源性。编码区在大肠杆菌中作为MS2聚合酶融合蛋白表达,该融合蛋白经纯化后用于免疫夜猴。用这种融合蛋白免疫的动物在感染恶性疟原虫后仅表现出低寄生虫血症(低于2%),而对照组动物或用携带其他疟疾特异性序列的MS2融合蛋白免疫的动物则未受到保护。结果表明,这种抗原是疟疾疫苗的良好候选物。