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Assembly of the vesicular stomatitis virus envelope transfer of viral poly peptides from polysomes to cellular membranes

Assembly of the vesicular stomatitis virus envelope transfer of viral poly peptides from polysomes to cellular membranes

Virology 76(1): 98-108

The lipoprotein envelope of vesicular stomatitis virus contains 2 polypeptides, M and G. Both are inserted into the host cell plasma membrane and are incorporated into virions as the nucleocapsid buds from the cell surface. These experiments concern the transfer of newly synthesized M and G polypeptide chains from polysomes to the plasma membrane. Infected [human amniotic U] cells were pulse-labeled for 2 min with radioactive amino acids to label completed M and G molecules and their nascent chains. Nascent M chains were associated with soluble polysomes, while nascent G chains were associated with membrane-bound polysomes. Completed G polypeptide chains were found exclusively in the cytoplasmic membrane fraction, while completed M chains were found in the membrane fraction and the postribosomal supernatant. These radioactive M polypeptide chains disappeared from the supernatant upon further incubation with nonradioactive amino acids. If pulse-labeled cells were incubated with puromycin so that polysomes were dissociated, nascent G peptide chains remained associated with the cytoplasmic membrane fraction. Newly synthesized M polypeptides are probably released into the soluble phase of the cytoplasm before reaching the plasma membrane, while newly synthesized G polypeptides may pass directly from membrane-bound polysomes to the membranes of the endoplasmic reticulum system. The G polypeptide appears to become membrane-associated prior to peptide chain completion.

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Accession: 004785982

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PMID: 189501

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