Post-translational processing and oligomerization of the fusion glycoprotein of human respiratory syncytial virus

The post-translational maturation of the fusion protein (F) of human respiratory syncytial virus was investi-gated. Chemical cross-linking experiments indicated that F forms homotetramers and provided evidence that the intermonomer contacts involve primarily the F1 subunit. Homooligomerization as measured by sedi-mentation in sucrose gradients was insensitive to car-bonyl cyanide m-chlorophenylhydrazone, indicating that it occurs in the endoplasmic reticulum. Cleavage of the F0 precursor to yield the FI and F 2 subunits was blocked by monensin or brefeldin A, indicating that it takes place in distal cisternae of the trans Golgi compartment or in the more distal trans Golgi network. The Fo precursor was not detected at the cell surface in surface immunoprecipitation experiments