Intracellular processing of measles virus fusion protein.

Intracellular processing of measles virus fusion (F) protein was studied by radiolabeling and immunoprecipitation with a monoclonal antibody against F protein. The cleavage of F protein into F1 and F2 subunits was complete after 5 hours of chase during which the growth of oligosaccharide chains on the F2 domain of F protein continued. The addition of terminal sialic acid conferred a strong negative charge on the F2 subunit. F protein expressed on the cell surface was removed by a fungal semi-alkaline protease, providing a method to follow the kinetics of its transport to the cell surface. The transport of the F protein was faster than that of the hemagglutinin (HA) protein. Uncleaved F protein, as well as cleaved subunits became digestible by the protease, indicating that a portion of the F protein reaches the cell surface uncleaved. The treatment of measles virus-infected cells with tunicamycin resulted in the synthesis of unglycosylated HA (65 kilodaltons, Kd) and F (48 Kd) proteins. Unglycosylated F protein was not cleaved into smaller subunits, nor was it transported to the cell surface. Unglycosylated HA protein likewise failed to reach the cell surface.