Crump C E, Arruda E, Hayden F G
Department of Internal Medicine, University of Virginia School of Medicine, Charlottesville 22908.
Antimicrob Agents Chemother. 1994 Jun;38(6):1425-7. doi: 10.1128/AAC.38.6.1425.
We conducted a comparative study of the antirhinovirus activities of soluble intercellular adhesion molecule-1 (sICAM-1) and a chimeric ICAM-1/immunoglobulin A (IgA) molecule (ICI-5D/IgA) for nine major receptor group human rhinovirus (HRV) serotypes and for a variant of HRV-39 relatively resistant to inhibition by sICAM-1. ICI-5D/IgA inhibited the infectivity of eight of the nine wild-type HRVs and the resistant HRV-39 variant and was 60 to 170 times more potent than sICAM-1 on a molar basis. In contrast to sICAM-1, ICI-5D/IgA directly neutralized the infectivity of the representative HRVs by approximately 1 log10. These results expand on the antirhinovirus spectrum of ICI-5D/IgA, confirm that dimeric forms of sICAM-1 have a higher antirhinoviral potency than monomeric sICAM-1, and indicate that cross-linking of two adjacent receptor binding sites on the virus capsid by a divalent receptor enhances the direct inactivation of viral infectivity.
我们对可溶性细胞间黏附分子-1(sICAM-1)和嵌合ICAM-1/免疫球蛋白A(IgA)分子(ICI-5D/IgA)针对9种主要受体组人鼻病毒(HRV)血清型以及对sICAM-1抑制相对耐药的HRV-39变异体的抗鼻病毒活性进行了比较研究。ICI-5D/IgA抑制了9种野生型HRV中的8种以及耐药的HRV-39变异体的感染性,在摩尔基础上其效力比sICAM-1高60至170倍。与sICAM-1不同,ICI-5D/IgA直接使代表性HRV的感染性中和约1个对数级。这些结果扩展了ICI-5D/IgA的抗鼻病毒谱,证实sICAM-1的二聚体形式比单体sICAM-1具有更高的抗鼻病毒效力,并表明通过二价受体使病毒衣壳上两个相邻受体结合位点交联可增强病毒感染性的直接失活。