摘要
对柯萨奇B4病毒(CVB4)衣壳蛋白VPl保守区的亲水性和二级结构进行分析和预测,选择可能代表优势抗原表位的肽段进行合成(VPl-l肽,RIYF KPKHVK AYV),并截取了该肽段的前12个残基(VPI-2肽)用同样方法进行合成.用VP1-1肽免疫家兔制备出高效价抗体,应用酶联免疫吸附法(ELISA)检测,这些抗体与CVBI-6病毒均有结合反应,VP1-1肽与型特异性CVB1-6抗体均有良好的结合反应,表明VP1-1肽是CVB的共同抗原表位.用VP1-1肽检测心肌炎患者血清CVBIgM抗体,阳性率在40%左右.
The conserved regions of CVB4 coat protein VP1 were analyzed and predicted for the hydrophilicity and secondary structure. Peptides representing potential antigenic domains were synthesized on soild-phase resins (VPl-1 peptide: RIYFKPKHVKAYV) .The first 12 residues (VP1-2 peptide) of this peptide was truncated and synthesized by the same method. VPl-1 peptide elicited strong antibody responses in rabbits. These antibodies recognized CVB1-6 viruses in enzyme-linked immunosorbent assays (ELISA) .When type-specific sera against CVB1-6 were tested in ELISA for binding to the synthetic peptides, it was found that all the six anti-CVB sera excellently bound to VPl-1 peptide, indicating that VPl-1 peptide was a common immunodominant domain of CVB. Detecting of IgM antibodies to Coxsackie B viruses in viral myocarditis by using VPl-1 peptide revealed that the positive rate was about 40%.
出处
《上海免疫学杂志》
CSCD
北大核心
1998年第4期220-222,共3页
Shanghai Journal of Immunology
基金
卫生部科学研究基金资助
