McCray J, Werner G
Sandoz Forschungsinstitut, Vienna, Austria.
Nature. 1987;329(6141):736-8. doi: 10.1038/329736a0.
Recently, Rossman et al. have described the three-dimensional structure of a human rhinovirus. A possible host cell surface receptor binding site was identified with a cleft on each icosahedral face. Two highly conserved amino-acid sequences found in rhino-, polio-, and foot-and-mouth disease (FMD) viruses are located near the base of this site and could be important in maintaining its topology. We have prepared site-specific antibodies to two synthetic peptides which include these sequences. The antibodies bind to the predicted capsid proteins of rhinovirus and neutralize approximately 60% of 48 rhinovirus serotypes tested. These results could provide a route to a rhinovirus vaccine effective against most of the numerous serotypes of this virus.
最近,罗斯曼等人描述了一种人类鼻病毒的三维结构。在每个二十面体面上的一个裂隙处鉴定出了一个可能的宿主细胞表面受体结合位点。在鼻病毒、脊髓灰质炎病毒和口蹄疫病毒中发现的两个高度保守的氨基酸序列位于该位点底部附近,可能对维持其拓扑结构很重要。我们针对包含这些序列的两种合成肽制备了位点特异性抗体。这些抗体与鼻病毒预测的衣壳蛋白结合,并中和了所测试的48种鼻病毒血清型中的约60%。这些结果可能为研发一种能有效对抗该病毒众多血清型中大多数的鼻病毒疫苗提供一条途径。