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


     

J Gen Virol 53 (1981), 363-369; DOI 10.1099/0022-1317-53-2-363
© 1981 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 Urquidi, V.
Right arrow Articles by Esparza, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Urquidi, V.
Right arrow Articles by Esparza, J.
Agricola
Right arrow Articles by Urquidi, V.
Right arrow Articles by Esparza, J.

Protein Synthesis in Cells Infected with Bovine Rotavirus

V. Urquidi, E. Novo and J. Esparza{dagger}

Laboratorio de Biología de Virus Instituto Venezolano de Investigaciones, Científicas Apartado 1827, Caracas 1010A, Venezuela

Bovine rotavirus was found to multiply efficiently in LLC-MK2 cells, a continuous line of rhesus monkey kidney, with a growth cycle which was essentially completed within 9 h after infection. The presence of low concentrations of trypsin (10 µg/ml) in the virus inoculum was essential for infectivity. Polyacrylamide gel electrophoresis of infected cell extracts demonstrated the synthesis of at least eight virus-specific polypeptides 6 h post-infection with mol. wt. ranging from 102 x 103 to 29 x 103. Six polypeptides (about p102K, p91K, p84K, p45K, p37K and p34K) were identified as structural components of the virion. Two other polypeptides (p54K and p29K) were identified as non-structural components. The synthesis of non-structural polypeptides appeared to precede that of the structural proteins. Pulse-chase experiments showed only one minor post-translation modification of the virus-specified proteins, namely an increase in the mobility of the 29K polypeptide.

{dagger} Present address: Department of Microbiology and Immunology, Duke University Medical Center, Box 3020, Durham, North Carolina 27710, U.S.A.

Received 8 September 1980; accepted 8 December 1980.




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 © 1981 by the Society for General Microbiology.