ABSTRACT
The envelope of vesicular stomatitis virus (VSV) contains a single glycosylated protein species which has a molecular weight of approximately 67,000. This glycoprotein constitutes the spike-like projections from the viral envelope which are seen in electron micrographs of negatively-stained, purified virus preparations. The structure of the oligosaccharide moieties of the VSV glycoprotein has been elucidated by sequential chemical and enzymatic degradation. Addition of membrane vesicle preparations to cell-free systems synthesizing G protein leads to the synthesis of a partially glycosylated species with the same molecular weight as the partially glycosylated species observed after short pulses in infected cells. The VSV G protein forms the spikes or surface projections seen in electron micrographs of intact virions. This peripheral location of the glycoprotein gives it a central role in several of the physiological properties of the virus particles.
