Moser D, Doenhoff M J, Klinkert M Q
Zentrum für Molekulare Biologie, Universität Heidelberg, Germany.
Mol Biochem Parasitol. 1992 Apr;51(2):229-38. doi: 10.1016/0166-6851(92)90073-s.
A cDNA sequence encoding a Schistosoma mansoni egg antigen SmE16 was cloned in Escherichia coli. The 16-kDa polypeptide deduced from the nucleotide sequence is related to the calmodulin and troponin C gene families of calcium-binding proteins, and the most significant homology is displayed around the four calcium-binding sites. The antigen was expressed as a hybrid protein of the bacteriophage MS2 polymerase. The MS2-SmE16 fusion protein binds calcium, as demonstrated via ligand blotting with 45Calcium. The detection of antibodies to the purified recombinant egg antigen in sera of schistosomiasis patients opens up the possibility that it may be a useful candidate for the development of serodiagnostic assays. The function of the protein in the egg is presently unclear.
编码曼氏血吸虫卵抗原SmE16的cDNA序列在大肠杆菌中被克隆。从核苷酸序列推导的16 kDa多肽与钙调蛋白和肌钙蛋白C基因家族的钙结合蛋白相关，并且在四个钙结合位点周围显示出最显著的同源性。该抗原被表达为噬菌体MS2聚合酶的融合蛋白。通过用45钙进行配体印迹法证明，MS2-SmE16融合蛋白结合钙。在血吸虫病患者血清中检测针对纯化重组卵抗原的抗体，为其可能成为血清诊断检测开发的有用候选物开辟了可能性。该蛋白在卵中的功能目前尚不清楚。
