Iorio Ronald M, Melanson Vanessa R, Mahon Paul J
Program in Immunology & Virology, University of Massachusetts Medical School, Worcester, MA 01655, USA and Department of Molecular Genetics & Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA, Tel.: +1 508 856 5257, ,
Future Virol. 2009 Jul 1;4(4):335-351. doi: 10.2217/fvl.09.17.
The Paramyxoviridae are enveloped, negative-stranded RNA viruses, some of which recognize sialic acid-containing receptors, while others recognize specific proteinaceous receptors. The major cytopathic effect of paramyxovirus infection is membrane fusion-induced syncytium formation. Paramyxoviruses are unusual in that the receptor-binding and fusion-promoting activities reside on two different spike structures, the attachment and fusion glycoproteins, respectively. For most paramyxoviruses, this distribution of functions requires a mechanism by which the two processes can be linked for the promotion of fusion. This is accomplished by a virus-specific interaction between the two proteins. An increasing body of evidence supports the notion that members of this family of viruses utilize this glycoprotein interaction in different ways in order to mediate the regulation of the fusion protein activation, depending on the type of receptor utilized by the virus.
副粘病毒科是有包膜的负链RNA病毒,其中一些识别含唾液酸的受体,而另一些识别特定的蛋白质受体。副粘病毒感染的主要细胞病变效应是膜融合诱导的多核巨细胞形成。副粘病毒不同寻常之处在于,受体结合和促进融合的活性分别存在于两种不同的刺突结构,即附着糖蛋白和融合糖蛋白上。对于大多数副粘病毒来说,这种功能分布需要一种机制,通过该机制这两个过程可以联系起来以促进融合。这是通过两种蛋白质之间的病毒特异性相互作用来实现的。越来越多的证据支持这样一种观点,即该病毒家族的成员根据病毒利用的受体类型,以不同方式利用这种糖蛋白相互作用来介导融合蛋白激活的调节。