Závada J
J Gen Virol. 1982 Nov;63 (Pt 1):15-24. doi: 10.1099/0022-1317-63-1-15.
The assembly of virion surface glycoproteins by enveloped viruses appears to be both specific and non-specific. It is non-specific in the sense that, during a dual infection by various unrelated viruses, there is very common (if not universal) and efficient mixing of envelope glycoproteins from both genotypes in the progeny virions. However, it seems to be specific in the sense that non-viral, cell surface proteins are, in the main, recognized as alien and are excluded from incorporation into virions during budding. These findings suggest that all enveloped viruses may share an essentially common molecular mechanism for the specific assembly and budding of virus glycoproteins while at the same time incorporating a mechanism for the exclusion of glycoproteins of cellular origin. One of the simplest explanations for this phenomenon may be that virus envelope surface structures all evolved from a single ancestral virus.
包膜病毒对病毒粒子表面糖蛋白的组装似乎既有特异性又有非特异性。说它非特异性,是因为在多种不相关病毒的双重感染过程中,子代病毒粒子中来自两种基因型的包膜糖蛋白非常普遍(即便不是全部)且高效地混合在一起。然而,说它有特异性,是因为非病毒的细胞表面蛋白在很大程度上被视为异类,在出芽过程中被排除在病毒粒子的组装之外。这些发现表明,所有包膜病毒可能共享一种基本通用的分子机制,用于病毒糖蛋白的特异性组装和出芽,同时还纳入了一种排除细胞源糖蛋白的机制。对这一现象最简单的解释之一可能是,病毒包膜表面结构均从单一的始祖病毒进化而来。