THE NUCLEOCAPSID-BINDING SPIKE SUBUNIT E2 OF SEMLIKI-FOREST-VIRUS REQUIRES COMPLEX-FORMATION WITH THE E1 SUBUNIT FOR ACTIVITY

Alphaviruses, such as Semliki Forest virus (SFV), mature by budding at the plasma membrane (Phl) of infected cells and enter uninfected ones by a membrane fusion process in the endosomes, Both processes are dir ected by the p62/E2-E1 membrane protein heterodimer of the virus. The p62 protein, or its mature form E2, provides a cytoplasmic protein dom ain for interaction with the nucleocapsid (NC) of the virus, and the F l protein functions as a membrane fusogen. We have previously shown th at the p62/E2 protein of SFV controls the membrane fusion activity of El through its complex formation with the latter (A, Salminen, J. hi. Wahlberg, M. Lobigs, P. Liljestrom, and H. Garoff, J. Cell Biol, 116:3 39-357, 1992). In the present work, we show that the El protein contro ls the NC-binding activity of p62/E2. We have studied E1 expression-de ficient SFV variants and shown that although the p62/EZ proteins can b e transported to the PR I they cannot establish stable NC associations .