Molecular mechanism of the paramyxovirus-mediated membrane fusion as analyzed by novel procedures for detection

副流感病毒5和猿猴病毒41的F蛋白嵌合分析显示，F蛋白头区表面的5个结构域中有21个氨基酸参与了与HN蛋白柄区的功能相互作用，从而诱导细胞-细胞融合。此外，这表明这种功能相互作用依赖于HN柄区域的构象。另一方面，双分子荧光互补分析结果表明，HN与F蛋白之间的物理相互作用不仅依赖于F蛋白的蛋白水解裂解，还依赖于F蛋白的构象变化。然而，有人认为，在生理条件下，他的物理相互作用是微弱的，其贪婪或发生非常短暂。

Chimeric analysis of the F proteins of the parainfluenza virus 5 and simian virus 41 revealed that 21 amino acids in the five domains on the surface of the F protein head region are involved in functional interaction with the HN protein stalk region, leading to the induction of cell-cell fusion. Furthermore, it was suggested that this functional interaction is dependent on the conformation of the HN stalk region.On the other hand, the results obtained from bimolecular fluorescence complementation analysis indicated that physical interaction between HN and F protein is not only dependent on the proteolytic cleavage of the F protein but also on the conformational change of the F protein. However, it was suggested that under physiological conditions his physical interaction is weak in its avidity or takes place very transiently.