The budding mechanism of spikeless vesicular stomatitis virus particles.
Virus particles, lacking the spike G-glycoproteins, are produced during infection of Vero cells with the vesicular stomatitis virus mutant ts045 at the restrictive temperature 39.5 degrees C. At this temperature the mutated G proteins are blocked in their intracellular transport in the endoplasmic reticulum. We have studied the role of the G proteins in the formation of these spikeless virus particles. The results showed that the spikeless particles contain a full complement of membrane anchors, derived from the carboxy-terminal end of the G protein. Our observations suggest that virus particles are formed at the restrictive temperature with G protein which is later cleaved to produce spikeless particles. We suggest that this is due to a leak of G protein to the cell surface at 39.5 degrees C where budding then takes place, presumably driven by a G protein C-terminal tail--nucleocapsid interaction.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000502:physiology; D002522:Chlorocebus aethiops; D003545:Cysteine / Q000378:metabolism; D007668:Kidney; D007700:Kinetics; D008562:Membrane Glycoproteins; D008715:Methionine / Q000378:metabolism; D010743:Phospholipids / Q000032:analysis; D011991:Receptors, Virus / Q000502:physiology; D013462:Sulfur Radioisotopes; D013696:Temperature; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics / Q000502:physiology*; D014759:Viral Envelope Proteins; D014764:Viral Proteins / Q000502:physiology*; D014771:Virion / Q000235:genetics / Q000502:physiology
C028391:G protein, vesicular stomatitis virus; D008562:Membrane Glycoproteins; D010743:Phospholipids; D011991:Receptors, Virus; D013462:Sulfur Radioisotopes; D014759:Viral Envelope Proteins; D014764:Viral Proteins; D008715:Methionine; D003545:Cysteine