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


     


J Gen Virol 47 (1980), 301-310; DOI 10.1099/0022-1317-47-2-301
© 1980 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 Robbins, S. J.
Right arrow Articles by Rapp, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Robbins, S. J.
Right arrow Articles by Rapp, F.
Agricola
Right arrow Articles by Robbins, S. J.
Right arrow Articles by Rapp, F.

Isolation and Partial Characterization of Two Forms of Cytoplasmic Nucleocapsids from Measles Virus-infected Cells

Steven J. Robbins, Robert H. Bussell* and Fred Rapp{dagger},{dagger}

Department of Microbiology, University of Kansas, Lawrence, Kansas 66044
{dagger} Department of Microbiology, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033, U.S.A.

Two species of measles virus nucleocapsids with distinct buoyant densities were isolated from infected AV3 cell homogenates by isopycnic CsCl gradient centrifugation. The more buoyant or ‘light’ form of the nucleocapsid had a density of 1.26 to 1.28 g/ml, whereas the less buoyant or ‘heavy’ nucleocapsid species had a density of 1.30 g/ml. Analysis of the two nucleocapsid species by SDS-polyacrylamide gel electrophoresis showed that both forms possessed two phosphorylated polypeptides with mol. wt. of 69000 and 60000. The heavy form of nucleocapsid consisted solely of these two polypeptide species, while the light form of nucleocapsid had two additional associated polypeptides (VP4, mol. wt. 52000, and 45K, mol. wt. 45000). Ultrastructural and immunofluorescent studies suggest that the two isolated capsid forms represent the two morphologically distinct capsid species observed in vivo. This paper discusses the possible relationship between the two capsid forms and assembly of the virus.

* Deceased.

{dagger} Author to whom correspondence should be addressed.

Received 11 July 1979; accepted 18 October 1979.


This article has been cited by other articles:


Home page
Protein Sci.Home page
J.-M. Bourhis, V. Receveur-Brechot, M. Oglesbee, X. Zhang, M. Buccellato, H. Darbon, B. Canard, S. Finet, and S. Longhi
The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
Protein Sci., August 1, 2005; 14(8): 1975 - 1992.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
C. L. Parks, R. A. Lerch, P. Walpita, M. S. Sidhu, and S. A. Udem
Enhanced Measles Virus cDNA Rescue and Gene Expression after Heat Shock
J. Virol., May 1, 1999; 73(5): 3560 - 3566.
[Abstract] [Full Text]




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 © 1980 by the Society for General Microbiology.