Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid.

摘要: The two envelope glycoproteins and the viral nucleocapsid of coronavirus A59 were isolated by solubilization membrane with Nonidet P-40 at 4 degrees C followed sucrose density gradient sedimentation. Isolated E2 consisted rosettes peplomers, whereas E1, glycoprotein, was irregular amorphous. Under certain conditions significant interactions occurred between components P-40-disrupted virions. Incubation virus 37 resulted in formation a complex one glycoproteins, nucleocapsid. This caused temperature-dependent conformational change resulting aggregation E1 interaction RNA also bound rRNA. E1-nucleocapsid complexes can be distinguished on Renografin gradients from native nucleocapsids. separation glycoprotein peplomeric permitted preparation antisera against these proteins. A model is proposed for arrangement three major structural proteins virion relation to RNA. Images