IMMUNOLOGY AND BIOLOGY OF RHINOVIRUSES

这里报道的研究是一个项目的一部分，该项目旨在确定 可用于将鼻病毒血清型分组的鼻病毒 具有共同的免疫决定因素和生物功能。来源的抗血清 针对个别人鼻病毒(HRV)血清型免疫的豚鼠 以前用来确定免疫印迹系统中的交叉反应 2型和14型HRV衣壳表面多肽(VP1、VP2、VP3) 和HRV14)在酶免疫分析中研究了类似的反应性 (环评)。对于EIA，鼻病毒的纯化采用CsCl梯度和贴壁法 以标准方法使用碳酸盐缓冲液至96井板。稀释 免疫豚鼠的抗血清与处理后的抗体发生反应。 平板，鼻病毒抗原特异性抗体的结合是 经碱性磷酸酶结合的豚鼠抗血清鉴定。这是 环评的初步结果与之前在#年发现的结果相似 免疫印迹。反应的HRV2、HRV1B和HRV89的抗血清 在免疫印迹中与HRV2强反应，在EIA中也与HRV2强反应。 免疫印迹法检测与HRV2无反应的HRV31抗血清 在EIA中也不与HRV2反应。其他血清型特异性抗血清 免疫印迹中与HRV2反应较弱的为中间激活 在环评中。反应性的模式与 免疫印迹结果和明确的HRV易感性谱 与相对保守的氨基酸结合的抗病毒化学物质的血清型 VP1衣壳表面有一个折叠的酸性序列。这些数据是 与免疫原性抗原决定簇的保守性一致。

The studies reported here are part of a program to identify properties of rhinoviruses which might be used to place rhinovirus serotypes into groups with shared immunologic determinants and biologic functions. Antisera from guinea pigs immunized against individual human rhinovirus (HRV) serotypes previously used to determine cross-reactivity in an immunoblot system with the capsid surface peptides (VP1, VP2, VP3) of HRV serotypes 2 and 14 (HRV2 and HRV14)) were studied for similar reactivity in an enzyme immunoassay (EIA). For the EIA rhinoviruses were purified by CsCl gradient and attache to 96 well plates using carbonate buffer in a standard method. Dilutions of antisera from the immunized guinea pigs were reacted with the treated plates, and the binding of antibodies specific for rhinovirus antigens was identified by anti-guinea pig sera conjugated with alkaline phosphatase. Th preliminary results of the EIA paralleled the results previously found in immunoblots. Antisera specific for HRV2, HRV1B, and HRV89 which reacted strongly with HRV2 in immunoblot also reacted strongly with HRV2 in EIA. Antisera specific for HRV31 which was unreactive with HRV2 in immunoblot wa also unreactive with HRV2 in EIA. Antisera specific for other serotypes which reacted weakly with HRV2 in immunoblot were intermediate in reactivit in EIA. The pattern of reactivity was consistent with the correlation of immunoblot results and defined spectrum of susceptibility of the HRV serotypes to antiviral chemicals which bind to a relatively conserved amino acid sequence occupying a fold in the capsid surface of VP1. The data are consistent with conservation of immunogenic antigenic determinants.