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Journal of Virology, March 2006, p. 3071-3077, Vol. 80, No. 6
0022-538X/06/$08.00+0 doi:10.1128/JVI.80.6.3071-3077.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Department of Biochemistry, Molecular Biology, and Cell Biology,1 Howard Hughes Medical Institute, Northwestern University, Evanston, Illinois 60208,2 School of Biomedical Sciences, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife, Scotland KY16 9TS, United Kingdom3
Received 8 December 2005/ Accepted 14 December 2005
Paramyxoviruses enter cells by fusing their envelopes with the plasma membrane, a process that occurs at neutral pH. Recently, it has been found that there is an exception to this dogma in that a porcine isolate of the paramyxovirus parainfluenza virus 5 (PIV5), known as SER, requires a low-pH step for fusion (S. Seth, A. Vincent, and R. W. Compans, J. Virol. 77: 6520-6527, 2003). As a low-pH activation mechanism for fusion would greatly facilitate biophysical studies of paramyxovirus-mediated membrane fusion, we have reexamined the triggering of the PIV5 SER fusion protein. Using multiple assays, we could not find a requirement for low-pH triggering of PIV5 SER fusion. The challenge of discovering how the paramyxovirus receptor binding protein (HN, H, or G) activates the metastable fusion protein to cause membrane fusion at neutral pH remains.
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