Intracellular processing of mumps virus glycoproteins

Abstract

Using newly isolated monoclonal antibodies (MoAb) directed to the hemagglutinin-neuraminidase (HN) and the fusion (F) glycoproteins of mumps virus, we have analyzed post-translational modification of both glycoproteins. The HN glycoprotein synthesized as a monomer slowly acquires immunoreactivity with a monoclonal antibody (MoAb) to the HN in conjunction with the formation of oligomers. The oligomerization of the HN protein appeared to take place during transport of the protein through the Golgi apparatus. The immunoreactivity of the F protein evolved quickly in the rough endoplasmic reticulum, and the precursor of the F protein appeared to be proteolytically cleaved into F1 and F2 at the trans Golgi cisternae.