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פותח על ידי קלירמאש פתרונות בע"מ -
Membrane vesicles containing the sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidylserine liposomes at low pH
Year:
1986
Source of publication :
Biochemistry (source )
Authors :
צ'חנובסקי, נור
;
.
Volume :
25
Co-Authors:
Chejanovsky, N., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Zakai, N., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Amselem, S., Department of Membrane Biochemistry and Neurochemistry, Hadassah Medical School, 91120 Jerusalem, Israel
Barenholz, Y., Department of Membrane Biochemistry and Neurochemistry, Hadassah Medical School, 91120 Jerusalem, Israel
Loyter, A., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Facilitators :
From page:
4810
To page:
4817
(
Total pages:
8
)
Abstract:
Membrane vesicles containing the Sendai virus hemagglutinin/neuraminidase (HN) glycoprotein were able to induce carboxyfluorescein (CF) release from loaded phosphatidylserine (PS) but not loaded phosphatidylcholine (PC) liposomes. Similarly, fluorescence dequenching was observed only when HN vesicles, bearing self-quenched N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine (N-NBD-PE), were incubated with PS but not PC liposomes. Thus, fusion between Sendai virus HN glycoprotein vesicles and the negatively charged PS liposomes is suggested. Induction of CF release and fluorescence dequenching were not observed when Pronase-treated HN vesicles were incubated with the PS liposomes. On the other hand, the fusogenic activity of the HN vesicles was not inhibited by treatment with dithiothreitol (DTT) or phenylmethanesulfonyl fluoride (PMSF), both of which are known to inhibit the Sendai virus fusogenic activity. Fusion was highly dependent on the pH of the medium, being maximal after an incubation of 60-90 s at pH 4.0. Electron microscopy studies showed that incubation at pH 4.0 of the HN vesicles with PS liposomes, both of which are of an average diameter of 150 nm, resulted in the formation of large unilamellar vesicles, the average diameter of which reached 450 nm. The relevance of these observations to the mechanism of liposome-membrane and virus-membrane fusion is discussed. © 1986 American Chemical Society.
Note:
Related Files :
Animals
chick embryo
Hemagglutinins, Viral
Kinetics
pH
Phosphatidylserines
virus fusion protein
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
25051
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:12
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Scientific Publication
Membrane vesicles containing the sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidylserine liposomes at low pH
25
Chejanovsky, N., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Zakai, N., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Amselem, S., Department of Membrane Biochemistry and Neurochemistry, Hadassah Medical School, 91120 Jerusalem, Israel
Barenholz, Y., Department of Membrane Biochemistry and Neurochemistry, Hadassah Medical School, 91120 Jerusalem, Israel
Loyter, A., Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Jerusalem, Israel
Membrane vesicles containing the sendai virus binding glycoprotein, but not the viral fusion protein, fuse with phosphatidylserine liposomes at low pH
Membrane vesicles containing the Sendai virus hemagglutinin/neuraminidase (HN) glycoprotein were able to induce carboxyfluorescein (CF) release from loaded phosphatidylserine (PS) but not loaded phosphatidylcholine (PC) liposomes. Similarly, fluorescence dequenching was observed only when HN vesicles, bearing self-quenched N-(7-nitro-2,1,3-benzoxadiazol-4-yl)phosphatidylethanolamine (N-NBD-PE), were incubated with PS but not PC liposomes. Thus, fusion between Sendai virus HN glycoprotein vesicles and the negatively charged PS liposomes is suggested. Induction of CF release and fluorescence dequenching were not observed when Pronase-treated HN vesicles were incubated with the PS liposomes. On the other hand, the fusogenic activity of the HN vesicles was not inhibited by treatment with dithiothreitol (DTT) or phenylmethanesulfonyl fluoride (PMSF), both of which are known to inhibit the Sendai virus fusogenic activity. Fusion was highly dependent on the pH of the medium, being maximal after an incubation of 60-90 s at pH 4.0. Electron microscopy studies showed that incubation at pH 4.0 of the HN vesicles with PS liposomes, both of which are of an average diameter of 150 nm, resulted in the formation of large unilamellar vesicles, the average diameter of which reached 450 nm. The relevance of these observations to the mechanism of liposome-membrane and virus-membrane fusion is discussed. © 1986 American Chemical Society.
Scientific Publication
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