J Gen Virol Tips for Better Browsing
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 66 (1985), 987-1000; DOI 10.1099/0022-1317-66-5-987
© 1985 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 Roux, L.
Right arrow Articles by Portner, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Roux, L.
Right arrow Articles by Portner, A.
Agricola
Right arrow Articles by Roux, L.
Right arrow Articles by Portner, A.

Three Variations in the Cell Surface Expression of the Haemagglutinin-Neuraminidase Glycoprotein of Sendai Virus

Laurent Roux, Pascale Beffy and Allen Portner1

Department of Microbiology, University of Geneva, C.M.U., 9 avenue de Champel, 1211 Geneva 4, Switzerland
and1 Division of Virology and Molecular Biology, St Jude Children's Research Hospital, Memphis, Tennessee, U.S.A.

The fate of the haemagglutinin-neuraminidase glycoprotein (HN) of Sendai virus in three types of infection was studied by measuring its sensitivity to endoglycosidase H and its rate of appearance and turnover at the cell surface. HN behaved differently in the three types of infection. When highly expressed at the surface, as in a lytic standard virus infection, HN accumulated at the surface in a stable form (half-life of disappearance from the surface » 10 h). When moderately expressed, as in a non-lytic standard virus plus defective interfering virus infection, HN reached the membrane normally, but turned over rapidly (half-life about 2 h) and was re-internalized. When poorly expressed, as in long-term persistent infection, HN did not reach the cell surface and appeared to be degraded before reaching it. In contrast to HN, the other viral glycoprotein, F0, exhibited a similar turnover rate at the cell surface in the three situations. However, when compared to surface expression in standard virus-infected cells under standardized conditions, F0 surface expression in persistently infected cells was reduced. This reduction correlates with a decreased maturation rate in these cells.

Keywords: Sendai virus, HN, persistent infection

Received 1 November 1984; accepted 15 January 1985.


This article has been cited by other articles:


Home page
J. Virol.Home page
C. Vogt, M. Eickmann, S. Diederich, M. Moll, and A. Maisner
Endocytosis of the Nipah Virus Glycoproteins
J. Virol., March 15, 2005; 79(6): 3865 - 3872.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Moll, H.-D. Klenk, G. Herrler, and A. Maisner
A Single Amino Acid Change in the Cytoplasmic Domains of Measles Virus Glycoproteins H and F Alters Targeting, Endocytosis, and Cell Fusion in Polarized Madin-Darby Canine Kidney Cells
J. Biol. Chem., May 18, 2001; 276(21): 17887 - 17894.
[Abstract] [Full Text] [PDF]




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 © 1985 by the Society for General Microbiology.