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Published online
doi:10.1083/jcb.200809175
The Journal of Cell Biology, Vol. 183, No. 2, 177-179
The Rockefeller University Press, 0021-9525 $30.00
© Harrison
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The pH sensor for flavivirus membrane fusion



Stephen C. Harrison

Howard Hughes Medical Institute and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115

Correspondence to Stephen C. Harrison: harrison{at}crystal.harvard.edu

Viruses that infect cells by uptake through endosomes have generally evolved to "sense" the local pH as part of the mechanism by which they penetrate into the cytosol. Even for the very well studied fusion proteins of enveloped viruses, identification of the specific pH sensor has been a challenge, one that has now been met successfully, for flaviviruses, by Fritz et al. (Fritz, R., K. Stiasny, and F.X. Heinz. 2008. J. Cell Biol. 183:353–361) in this issue. Thorough mutational analysis of conserved histidine residues in the envelope protein of tick-borne encephalitis virus led Fritz et al. (2008) to identify a histidine at a key domain interface as the critical pH sensor; its protonation triggers the large-scale conformational rearrangement that induces fusion of viral and endosomal membranes.

© 2008 Harrison This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).


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Related Article

Identification of specific histidines as pH sensors in flavivirus membrane fusion
Richard Fritz, Karin Stiasny, and Franz X. Heinz
J. Cell Biol. 2008 183: 353-361. [Abstract] [Full Text] [PDF]





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