Tomassini J E, Colonno R J
J Virol. 1986 May;58(2):290-5. doi: 10.1128/JVI.58.2.290-295.1986.
Human rhinoviruses can be classified into major and minor groups on the basis of receptor specificity. Recently, a mouse monoclonal antibody was isolated which selectively blocked the attachment of the major group of human rhinoviruses to cells. Using this monoclonal antibody, the cellular receptor for the major group of human rhinoviruses was isolated. A radioimmunoassay was developed by using the receptor antibody to specifically detect rhinovirus receptor during isolation. Solubilized receptor from detergent-treated HeLa cell membrane extracts eluted from gel filtration columns with an apparent molecular weight of 440,000. A cellular receptor protein, which had a molecular weight of 90,000 when analyzed on sodium dodecyl sulfate-polyacrylamide gels, was purified from solubilized extracts on an immunoaffinity column containing receptor antibody. Polyclonal rabbit antiserum, resulting from immunization with the isolated receptor protein, specifically blocked the attachment of the major group of human rhinoviruses and indicated that the 90-kilodalton protein plays a functional role in attachment. Prolonged exposure of HeLa cell monolayers with the receptor antibody showed no inhibition of cell growth and division.
人鼻病毒可根据受体特异性分为主要组和次要组。最近,分离出一种小鼠单克隆抗体,它能选择性地阻断主要组人鼻病毒与细胞的附着。利用这种单克隆抗体,分离出了主要组人鼻病毒的细胞受体。通过使用受体抗体开发了一种放射免疫测定法,用于在分离过程中特异性检测鼻病毒受体。从经去污剂处理的HeLa细胞膜提取物中溶解的受体从凝胶过滤柱上洗脱下来,表观分子量为440,000。在含有受体抗体的免疫亲和柱上,从溶解提取物中纯化出一种细胞受体蛋白,该蛋白在十二烷基硫酸钠-聚丙烯酰胺凝胶上分析时分子量为90,000。用分离出的受体蛋白免疫产生的兔多克隆抗血清特异性地阻断了主要组人鼻病毒的附着,表明90千道尔顿的蛋白在附着过程中起功能性作用。用受体抗体长时间处理HeLa细胞单层未显示对细胞生长和分裂的抑制作用。