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• W1540371109 startingPage "10392" @default.
• W1540371109 abstract "The fusion of Sendai virus at pH 4-7 with artificial lipid vesicles composed of phosphatidylserine or phosphatidylcholine was quantified by measuring fluorescence energy transfer from N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-phosphatidylethanolamine to N-(lissamine-rhodamine-B-sulfonyl)-phosphatidylethanolamine in the target membranes. About 60% of the phosphatidylserine vesicles and virus appeared to fuse at pH 4 and about 100% at pH 5. Fusion was much less under all other conditions. The apparent fusion at pH 4, however, was due to a decrease in absorption of the acceptor probe, instead of dilution of acceptor as a result of fusion of labeled vesicles with unlabeled virus. After correction for this fusion-independent effect of Sendai virus, the extent of fusion was only 4-20% at pH 4 but still 80-100% at pH 5. These findings paralleled the loss of hemagglutinating and hemolytic activities of the virus induced by incubation at pH 4 but not at pH 5. Vesicle-virus hybrids were observed with the electron microscope after incubation at pH 5 but not at pH 7. The assay of membrane fusion by fluorescence energy transfer can be misleading unless correction is made for changes in energy transfer due to fusion-independent effects." @default.
• W1540371109 created "2016-06-24" @default.
• W1540371109 creator A5065593045 @default.
• W1540371109 date "1987-07-01" @default.
• W1540371109 modified "2023-10-17" @default.
• W1540371109 title "Energy transfer measurements of fusion between Sendai virus and vesicles corrected for decreased absorption of acceptor probe." @default.
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• W1540371109 doi "https://doi.org/10.1016/s0021-9258(18)61125-1" @default.
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