J Gen Virol Faster Access
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

J Gen Virol 17 (1972), 197-212; DOI 10.1099/0022-1317-17-2-197
© 1972 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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dobos, P.
Right arrow Articles by Martin, E. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dobos, P.
Right arrow Articles by Martin, E. M.
Agricola
Right arrow Articles by Dobos, P.
Right arrow Articles by Martin, E. M.

Virus-specific Polypeptides in Ascites Cells Infected with Encephalomyocarditis Virus

P. Dobos* and E. M. Martin{dagger}

National Institute for Medical Research, Mill Hill, London NW7 1AA, England

A study was made of the virus-specific proteins present in Krebs 2 ascites cells infected with encephalomyocarditis (EMC) virus. About 15 virus-specific polypeptides, mol. wt. varying from 13000 to 147000, were detected by acrylamide gel analysis of extracts from infected cells briefly pulsed with [14C]-amino acids. Three of the components were probably capsid proteins, while the fourth capsid protein (7300 mol. wt.) was not detected in the infected cell and possibly arose after maturation by cleavage of the largest capsid protein. Pulse-chase experiments showed that only two medium-sized (mol. wt. 36000 and 54000) and some smaller (mol. wt. 13500 to 17000) non-capsid proteins were stable in vivo; the remaining larger non-capsid proteins lost radioactivity during the chase with cold amino acids, and were probably intermediates in the formation of smaller polypeptides by some post-translational cleavage process. Various methods were employed to block this cleavage process, utilizing elevated temperatures, protease inhibitors and amino acid analogues.

* Present address: Department of Microbiology, Faculty of Medicine, Dalhousie University, Halifax, N.S., Canada.

{dagger} Present address: School of Biological Sciences, Flinders University, Bedford Park, South Australia 5042.

Received 24 April 1972; accepted 14 July 1972.




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 © 1972 by the Society for General Microbiology.