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J Virol. 1971 November; 8(5): 722-729
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Proteins of Vesicular Stomatitis Virus and of Phenotypically Mixed Vesicular Stomatitis Virus-Simian Virus 5 Virions 1

James J. McSharry, Richard W. Compans and Purnell W. Choppin

The Rockefeller University, New York, New York 10021

ABSTRACT

The identity of the glycoprotein of vesicular stomatitis virus (VSV) as the spike protein has been confirmed by the removal of the spikes with a protease from Streptomyces griseus, leaving bullet-shaped particles bounded by a smooth membrane. This treatment removes the glycoprotein but does not affect the other virion proteins, apparently because they are protected from the enzyme by the lipids in the viral membrane. The proteins of phenotypically mixed, bullet-shaped virions produced by cells mixedly infected with VSV and the parainfluenza virus simian virus 5 (SV5) have been analyzed by polyacrylamide gel electrophoresis. These virions contain all the VSV proteins plus the two SV5 spike proteins, both of which are glycoproteins. The finding of the SV5 spike glycoproteins on virions with the typical morphology of VSV indicates that there is not a stringent requirement that only the VSV glycoprotein can be used to form the bullet-shaped virion. On the other hand, the SV5 nucleocapsid protein and the major non-spike protein of the SV5 envelope were not detected in the phenotypically mixed virions, and this suggests that a specific interaction between the VSV nucleocapsid and regions of the cell membrane which contain the nonglycosylated VSV envelope protein is necessary for assembly of the bullet-shaped virion.

FOOTNOTES

1 Presented at the 71st Annual Meeting of the American Society for Microbiology, Minneapolis, Minn., 2-7 May 1971.

J Virol. 1971 November; 8(5): 722-729
Copyright © 1971 American Society for Microbiology. All Rights Reserved.



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Copyright © 1971 by the American Society for Microbiology. All rights reserved.