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Published March 1977 | Published
Journal Article Open

Maturation of viral proteins in cells infected with temperature-sensitive mutants of vesicular stomatitis virus


Maturation of viral proteins in cells infected with mutants of vesicular stomatitis virus was studied by surface iodination and cell fractionation. The movement of G, M, and N proteins to the virion bud appeared to be interdependent. Mutations thought to be in G protein prevented its migration to the cell surface, allowed neither M nor N protein to become membrane bound, and blocked formation of viral particles. Mutant G protein appeared not to leave the endoplasmic reticulum at the nonpermissive temperature, but this defect was partially reversible. In cells infected with mutants that caused N protein to be degraded rapidly or prevented its assembly into nucleocapsids, M protein did not bind to membranes and G protein matured to the cell surface, but never entered structures with the density of virions. Mutations causing M protein to be degraded prevented virion formation, and G protein behaved as in cells infected by mutants in N protein. These results are consistent with a model of virion formation involving coalescence of soluble nucleocapsid and soluble M protein with G protein already in the plasma membrane.

Additional Information

© 1977 American Society for Microbiology. Received for publication 10 September 1976. We gratefully acknowledge the technical assistance of Martin Brock. D.K. was supported by a National Science Foundation predoctoral fellowship during part of this work and a Public Health Service traineeship during the remainder. D.B. is an American Cancer Society research professor. H.F.L. was the recipient of Public Health Service research career development award GM-50175 from the National Institute of General Medical Sciences. This work was supported by Public Health Service grants AI-08814 and AI-08388 from the National Institute of Allergy and Infectious Diseases, American Cancer Society grant E559, and Public Health Service grant CA-12174 from the National Cancer Institute.

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