Ayata M, Sugano T, Murayama T, Sakamuro D, Takegami T, Matsumoto Y, Furukawa T
Department of Microbiology, Kanazawa Medical University, Ishikawa, Japan.
J Med Virol. 1994 Aug;43(4):386-92. doi: 10.1002/jmv.1890430412.
The amino-terminal portion of human cytomegalovirus glycoprotein B (HCMV-gB) was expressed as a fusion protein to analyze the neutralizing epitope recognized by human monoclonal antibody C23 and the humoral immune response to this epitope. The linear neutralizing epitope was further localized to the peptide within 17 amino acids (position 68-84) which were conserved between two HCMV laboratory strains. Ten out of 17 HCMV-seropositive human sera contained the antibody against this epitope. Although seven sera were negative for reacting with the fusion protein, the viruses isolated from the same patients retained the epitope. The immunogenicity of the epitope and the possible application of C23 human monoclonal antibody for passive immunization against HCMV infections are discussed.
表达人巨细胞病毒糖蛋白B（HCMV-gB）的氨基末端部分作为融合蛋白，以分析人单克隆抗体C23识别的中和表位以及对该表位的体液免疫反应。线性中和表位进一步定位于两个HCMV实验室菌株之间保守的17个氨基酸（第68-84位）内的肽段。17份HCMV血清阳性的人血清中有10份含有针对该表位的抗体。尽管7份血清与融合蛋白反应呈阴性，但从同一患者分离的病毒保留了该表位。讨论了该表位的免疫原性以及C23人单克隆抗体在被动免疫预防HCMV感染中的可能应用。
