Duechler M, Ketter S, Skern T, Kuechler E, Blaas D
Institute of Biochemistry, Medical Faculty, University of Vienna, Austria.
J Gen Virol. 1993 Oct;74 ( Pt 10):2287-91. doi: 10.1099/0022-1317-74-10-2287.
Amino acid sequence comparisons between the capsid proteins of several human rhinovirus (HRV) serotypes identified residues potentially involved in the discrimination between the major and the minor group receptors. Amino acids conserved within minor group HRVs were substituted in a full-length cDNA clone of HRV2 for those found at equivalent positions in major group HRVs. Transfection of HeLa cells with RNAs transcribed from seven individual mutated cDNAs gave rise to only two viable viruses; growth characteristics and affinity for the minor group receptor of both were unchanged compared to wild-type. Similar mutations in HRV14 were previously shown to alter the affinity for its receptor; the contact sites between the minor group viruses and the respective receptor may therefore be different.
对几种人鼻病毒(HRV)血清型的衣壳蛋白进行氨基酸序列比较,确定了可能参与区分主要和次要组受体的残基。在HRV2的全长cDNA克隆中,将次要组HRV中保守的氨基酸替换为主要组HRV中相同位置发现的氨基酸。用从七个单独的突变cDNA转录的RNA转染HeLa细胞,仅产生了两种活病毒;与野生型相比,两者的生长特性和对次要组受体的亲和力均未改变。先前已证明HRV14中的类似突变会改变其对受体的亲和力;因此,次要组病毒与各自受体之间的接触位点可能不同。