Sato H, Hirata J, Furukawa M, Kuroda N, Shiraki H, Maeda Y, Okochi K
Clinical Laboratory, Kyushu University Hospital, Fukuoka, Japan.
J Virol. 1991 Apr;65(4):1667-72. doi: 10.1128/JVI.65.4.1667-1672.1991.
In this study, we identified a region in the human parvovirus structural protein which involves the neutralization of the virus by a monoclonal antibody and site-specific synthetic peptides. A newly established monoclonal antibody reacted with both viral capsid proteins VP1 and VP2. The epitope was found in six strains of independently isolated human parvovirus B19. The monoclonal antibody could protect colony-forming unit erythroid in human bone marrow cell culture from injury by the virus. The monoclonal antibody reacted with only 1 of 12 peptides that were synthesized according to a predicted amino acid sequence based on nucleotide sequences of the coding region for the structural protein of B19 virus. The sequence recognized by the antibody was a site corresponding to amino acids 328 to 344 from the amino-terminal portion of VP2. This evidence suggests that the epitope of the viral capsid protein is located on the surface of the virus and may be recognized by virus-neutralizing antibodies.
在本研究中，我们在人细小病毒结构蛋白中鉴定出一个区域，该区域涉及单克隆抗体和位点特异性合成肽对病毒的中和作用。一种新建立的单克隆抗体与病毒衣壳蛋白VP1和VP2均发生反应。在六株独立分离的人细小病毒B19中发现了该表位。该单克隆抗体可保护人骨髓细胞培养中的红系集落形成单位免受病毒损伤。该单克隆抗体仅与根据基于B19病毒结构蛋白编码区核苷酸序列预测的氨基酸序列合成的12种肽中的1种发生反应。抗体识别的序列是对应于VP2氨基末端部分氨基酸328至344的位点。这一证据表明，病毒衣壳蛋白的表位位于病毒表面，可能被病毒中和抗体识别。
