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Published March 1977 | Published
Journal Article Open

Localization of two cellular forms of the vesicular stomatitis viral glycoprotein


Two cell-associated forms of the glycoprotein (G) of vesicular stomatitis virus, termed G_1 and G_2, have been resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. G_1 has the higher electrophoretic mobility, but both forms migrate more slowly than G protein synthesized in a wheat germ cell-free system (G_0), which presumably is the unglycosylated form. G_1 is a kinetic precursor of the G_2 form, and the apparent cause of the electrophoretic difference between the two species is the presence of N-acetylneuraminic acid on the G_2 form. Conversion of G_1 to G_2 occurs 10 to 20 min prior to the appearance of the G_2 form of the protein on the cell surface. This suggests that the G protein may be completely glycosylated several minutes prior to its migration to the cell surface and that glycosylation is not the limiting step in its maturation. No glycoprotein comigrating with G_0 can be detected in the infected cells, even after 5-min labeling periods; this suggests that partial clycosylation of G occurs concomitantly with or immediately after its synthesis.

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 Al-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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