JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JVI.02266-07v1
82/6/3131    most recent
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 Delos, S. E.
Right arrow Articles by White, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Delos, S. E.
Right arrow Articles by White, J. M.

 Previous Article  |  Next Article 

Journal of Virology, March 2008, p. 3131-3134, Vol. 82, No. 6
0022-538X/08/$08.00+0     doi:10.1128/JVI.02266-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cysteines Flanking the Internal Fusion Peptide Are Required for the Avian Sarcoma/Leukosis Virus Glycoprotein To Mediate the Lipid Mixing Stage of Fusion with High Efficiency{triangledown}

Sue E. Delos,1*,{dagger} Matthew B. Brecher,2,{dagger} Zaoying Chen,1 Deborah C. Melder,3 Mark J. Federspiel,3 and Judith M. White1,2

Departments of Cell Biology,1 Microbiology and Immunology, The University of Virginia, Charlottesville, Virginia 22908,2 Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota 559053

Received 18 October 2007/ Accepted 20 December 2007

We previously showed that the cysteines flanking the internal fusion peptide of the avian sarcoma/leukosis virus subtype A (ASLV-A) Env (EnvA) are important for infectivity and cell-cell fusion. Here we define the stage of fusion at which the cysteines are required. The flanking cysteines are dispensable for receptor-triggered membrane association but are required for the lipid mixing step of fusion, which, interestingly, displays a high pH onset and a biphasic profile. Second-site mutations that partially restore infection partially restore lipid mixing. These findings indicate that the cysteines flanking the internal fusion peptide of EnvA (and perhaps by analogy Ebola virus glycoprotein) are important for the foldback stage of the conformational changes that lead to membrane merger.

* Corresponding author. Mailing address: Department of Cell Biology, UVA Health System, School of Medicine, P.O. Box 800732, Charlottesville, VA 22908-0732. Phone: (434) 924-2009. Fax: (434) 982-3912. E-mail: sed7a{at}virginia.edu

{triangledown} Published ahead of print on 9 January 2008.

{dagger} S.E.D. and M.B.B. contributed equally to this work.

Journal of Virology, March 2008, p. 3131-3134, Vol. 82, No. 6
0022-538X/08/$08.00+0     doi:10.1128/JVI.02266-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2008 by the American Society for Microbiology. All rights reserved.