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
Right arrow Citation Map
Services
Right arrow E-mail 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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Roche, S.
Right arrow Articles by Gaudin, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Roche, S.
Right arrow Articles by Gaudin, Y.

 Previous Article  |  Next Article 

Journal of Virology, August 2004, p. 8746-8752, Vol. 78, No. 16
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.16.8746-8752.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Evidence that Rabies Virus Forms Different Kinds of Fusion Machines with Different pH Thresholds for Fusion

Stéphane Roche and Yves Gaudin*

Laboratoire de Virologie Moléculaire et Structurale, CNRS, 91198 Gif sur Yvette Cedex, France

Received 11 February 2004/ Accepted 5 April 2004

Fusion of rabies virus with membranes is triggered at a low pH and is mediated by a viral glycoprotein (G). Fusion of rabies virus with liposomes was monitored by using a lipid mixing assay based on fluorescence resonance energy transfer. Fusion was detected below pH 6.4, and its extent increased with H+ concentrations to be maximal around pH 6.15. The origin of the partial fusion activity of rabies virus under suboptimal pH conditions (i.e., between pH 6.15 and 6.4) was investigated. We demonstrate unambiguously that fusion at a suboptimal pH is distinct from the phenomenon of low-pH-induced inactivation and that it is not due to heterogeneity of the virus population. We also show that viruses that do not fuse under suboptimal pH conditions are indeed bound to the target liposomes and that the fusion complexes they have formed are blocked at an early stage of the fusion pathway. Our conclusion is that along the fusion reaction, different kinds of fusion machines with different pH thresholds for fusion can be formed. Possible explanations of this difference of pH sensitivity are discussed.

* Corresponding author. Mailing address: Laboratoire de Virologie Moléculaire et Structurale, CNRS, 91198 Gif sur Yvette Cedex, France. Phone: 33 1 69 82 38 37. Fax: 33 1 69 82 43 08. E-mail: gaudin{at}vms.cnrs-gif.fr.

Journal of Virology, August 2004, p. 8746-8752, Vol. 78, No. 16
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.16.8746-8752.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Klingen, Y., Conzelmann, K.-K., Finke, S. (2008). Double-Labeled Rabies Virus: Live Tracking of Enveloped Virus Transport. J. Virol. 82: 237-245 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»