Lohmeyer J, Talens L T, Klenk H D
J Gen Virol. 1979 Jan;42(1):73-88. doi: 10.1099/0022-1317-42-1-73.
Synthesis and processing of the envelope proteins of influenza A virus (fowl plague virus) have been analysed in BHK, HeLa and L cells, in which the virus undergoes abortive replication and does not form virus particles, and in the productive chick embryo fibroblast system. In abortive infection, synthesis of the M protein is specifically inhibited. The extent of this defect varies depending on the host cell and the amount of virus particles formed closely reflects the amount of M synthesized. Cell fractionation experiments demonstrated that the haemagglutinin glycoprotein HA is synthesized in abortive as well as in productive cells at the rough endoplasmic reticulum, that it migrates via smooth internal membranes to the plasma membrane and that it is cleaved by proteolysis into fragments HA1 and HA2 in the course of migration. Immune electron microscopy using monospecific antibodies against haemagglutinin and neuraminidase showed that both glycoproteins are exposed at the cell surface. Thus, synthesis and processing of the virus glycoproteins does not depend on the formation of the M protein. However, the M protein appears to be necessary for budding and thus for particle formation.
甲型流感病毒（禽瘟病毒）包膜蛋白的合成与加工已在BHK、HeLa和L细胞中进行了分析，在这些细胞中病毒进行流产性复制且不形成病毒颗粒，同时也在有生产性的鸡胚成纤维细胞系统中进行了分析。在流产性感染中，M蛋白的合成受到特异性抑制。这种缺陷的程度因宿主细胞而异，形成的病毒颗粒数量密切反映了合成的M蛋白数量。细胞分级分离实验表明，血凝素糖蛋白HA在流产性感染细胞和有生产性的细胞中均在糙面内质网合成，它通过光滑内膜迁移至质膜，并在迁移过程中经蛋白水解裂解为片段HA1和HA2。使用针对血凝素和神经氨酸酶的单特异性抗体进行的免疫电子显微镜检查表明，两种糖蛋白均暴露于细胞表面。因此，病毒糖蛋白的合成与加工并不依赖于M蛋白的形成。然而，M蛋白似乎对于出芽从而对于颗粒形成是必需的。
