A Caltech Library Service

Localization of two cellular forms of the vesicular stomatitis viral glycoprotein

Knipe, David M. and Lodish, Harvey F. and Baltimore, David (1977) Localization of two cellular forms of the vesicular stomatitis viral glycoprotein. Journal of Virology, 21 (3). pp. 1121-1127. ISSN 0022-538X. PMCID PMC515653.

PDF - Published Version
See Usage Policy.


Use this Persistent URL to link to this item:


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.

Item Type:Article
Related URLs:
URLURL TypeDescription CentralArticle
Knipe, David M.0000-0003-1554-6236
Baltimore, David0000-0001-8723-8190
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.
Funding AgencyGrant Number
NSF Predoctoral FellowshipUNSPECIFIED
NIH Predoctoral FellowshipUNSPECIFIED
National Institute of General Medical SciencesUNSPECIFIED
American Cancer SocietyE559
Issue or Number:3
PubMed Central ID:PMC515653
Record Number:CaltechAUTHORS:20120802-083032069
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:32861
Deposited On:02 Aug 2012 19:20
Last Modified:28 Jan 2021 23:59

Repository Staff Only: item control page