J Gen Virol Try IJSEM Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 37 (1977), 75-83; DOI 10.1099/0022-1317-37-1-75
© 1977 Society for General Microbiology

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ponder, B. A. J.
Right arrow Articles by Crawford, L. V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ponder, B. A. J.
Right arrow Articles by Crawford, L. V.
Agricola
Right arrow Articles by Ponder, B. A. J.
Right arrow Articles by Crawford, L. V.

Phosphorylation of Polyoma and SV40 Virus Proteins

B. A. J. Ponder, A. K. Robbins and L. V. Crawford

Department of Molecular Virology, Imperial Cancer Research Fund, London WC2A 3PX

The polypeptides of polyoma and SV40 virions are phosphorylated. An estimate of the amount of phosphorylation of the major virus capsid protein (VP1) has been made using two-dimensional gel electrophoresis to resolve phosphorylated from non-phosphorylated forms. The results suggest that in both polyoma and SV40 virions about 12% of VP1 molecules are phosphorylated. In unassembled VP1 molecules immunoprecipitated from extracts of infected cells the proportion is greater, about 33%. The possibility that phosphorylated VP1 may form the penton proteins of the virus capsid is discussed.

Received 3 February 1977; accepted 27 April 1977.


This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
K An, E. Gillock, J. Sweat, W. Reeves, and R. Consigli
Use of the baculovirus system to assemble polyomavirus capsid-like particles with different polyomavirus structural proteins: analysis of the recombinant assembled capsid-like particles
J. Gen. Virol., April 1, 1999; 80(4): 1009 - 1016.
[Abstract]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1977 by the Society for General Microbiology.