This Article
Right arrow Full Text
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 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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Andersson, H.
Right arrow Articles by Garoff, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andersson, H.
Right arrow Articles by Garoff, H.

 Previous Article  |  Next Article 

Journal of Virology, June 2003, p. 6676-6682, Vol. 77, No. 12
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.12.6676-6682.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Lectin-Mediated Retention of p62 Facilitates p62-E1 Heterodimerization in Endoplasmic Reticulum of Semliki Forest Virus-Infected Cells

Helena Andersson* and Henrik Garoff

Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden

Received 22 November 2002/ Accepted 25 March 2003

The Semliki Forest virus (SFV) spike subunits p62 and E1 are made from a common coding unit in the order p62-E1. The proteins are separated by the host signal peptidase upon translocation into the endoplasmic reticulum (ER). Shortly thereafter, p62 and E1 form heterodimers. Heterodimerization preferentially occurs between subunits derived from the same translation product, so-called cis heterodimerization. As the p62 protein has the capacity to leave the ER in the absence of E1, it has been postulated that there exists a retention mechanism for the p62 protein, putatively at or near the translocon, in the ER in order to promote cis heterodimerization (B. U. Barth and H. Garoff, J. Virol. 71:7857-7865, 1997). Here we show that there exists such a mechanism, that it is at least in part mediated by the ER chaperones calnexin and calreticulin, and that the retention is important for efficient cis heterodimerization.

* Corresponding author. Mailing address: Department of Biosciences at Novum, Karolinska Institute, S-141 57 Huddinge, Sweden. Phone: 46-8-608 91 20/7. Fax: 46-8-774 55 38. E-mail: Helena.Andersson{at}biosci.ki.se.

Journal of Virology, June 2003, p. 6676-6682, Vol. 77, No. 12
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.12.6676-6682.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»