Abstract
The low pH-triggered membrane fusion activity of Semliki Forest virus is dependent on the presence of cholesterol in the target membrane. When liposomes containing phospholipids and cholesterol analogs were used, fusion activity was observed with steroids which did not have a planar nucleus or an isooctyl side chain at C-17, but fusion activity was not observed when analogs which lacked the 3 beta-OH group were used. Binding of virus to liposomes at low pH was similarly, but not totally, dependent on the presence of a 3 beta-OH sterol.
Full text
PDFSelected References
These references are in PubMed. This may not be the complete list of references from this article.
- Alouf J. E. Streptococcal toxins (streptolysin O, streptolysin S, erythrogenic toxin). Pharmacol Ther. 1980;11(3):661–717. doi: 10.1016/0163-7258(80)90045-5. [DOI] [PubMed] [Google Scholar]
- Bloch K. E. Sterol structure and membrane function. CRC Crit Rev Biochem. 1983;14(1):47–92. doi: 10.3109/10409238309102790. [DOI] [PubMed] [Google Scholar]
- Bruckdorfer K. R., Demel R. A., De Gier J., van Deenen L. L. The effect of partial replacements of membrane cholesterol by other steroids on the osmotic fragility and glycerol permeability of erythrocytes. Biochim Biophys Acta. 1969 Jul 15;183(2):334–345. doi: 10.1016/0005-2736(69)90089-3. [DOI] [PubMed] [Google Scholar]
- Demel R. A., Bruckdorfer K. R., van Deenen L. L. Structural requirements of sterols for the interaction with lecithin at the air water interface. Biochim Biophys Acta. 1972 Jan 17;255(1):311–320. doi: 10.1016/0005-2736(72)90030-2. [DOI] [PubMed] [Google Scholar]
- Demel R. A., Bruckdorfer K. R., van Deenen L. L. The effect of sterol structure on the permeability of lipomes to glucose, glycerol and Rb + . Biochim Biophys Acta. 1972 Jan 17;255(1):321–330. doi: 10.1016/0005-2736(72)90031-4. [DOI] [PubMed] [Google Scholar]
- Demel R. A., De Kruyff B. The function of sterols in membranes. Biochim Biophys Acta. 1976 Oct 26;457(2):109–132. doi: 10.1016/0304-4157(76)90008-3. [DOI] [PubMed] [Google Scholar]
- Erwin C., Brown D. T. Requirement of cell nucleus for Sindbis virus replication in cultured Aedes albopictus cells. J Virol. 1983 Feb;45(2):792–799. doi: 10.1128/jvi.45.2.792-799.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fisher K. A. Analysis of membrane halves: cholesterol. Proc Natl Acad Sci U S A. 1976 Jan;73(1):173–177. doi: 10.1073/pnas.73.1.173. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Geoffroy C., Alouf J. E. Selective purification by thiol-disulfide interchange chromatography of alveolysin, a sulfhydryl-activated toxin of Bacillus alvei. Toxin properties and interaction with cholesterol and liposomes. J Biol Chem. 1983 Aug 25;258(16):9968–9972. [PubMed] [Google Scholar]
- Gershfeld N. L. Equilibrium studies of lecithin-cholesterol interactions I. Stoichiometry of lecithin-cholesterol complexes in bulk systems. Biophys J. 1978 Jun;22(3):469–488. doi: 10.1016/S0006-3495(78)85500-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Helenius A., Kartenbeck J., Simons K., Fries E. On the entry of Semliki forest virus into BHK-21 cells. J Cell Biol. 1980 Feb;84(2):404–420. doi: 10.1083/jcb.84.2.404. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hsu M. C., Scheid A., Choppin P. W. Fusion of Sendai virus with liposomes: dependence on the viral fusion protein (F) and the lipid composition of liposomes. Virology. 1983 Apr 15;126(1):361–369. doi: 10.1016/0042-6822(83)90485-3. [DOI] [PubMed] [Google Scholar]
- Kundrot C. E., Spangler E. A., Kendall D. A., MacDonald R. C., MacDonald R. I. Sendai virus-mediated lysis of liposomes requires cholesterol. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1608–1612. doi: 10.1073/pnas.80.6.1608. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Maeda T., Kawasaki K., Ohnishi S. Interaction of influenza virus hemagglutinin with target membrane lipids is a key step in virus-induced hemolysis and fusion at pH 5.2. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4133–4137. doi: 10.1073/pnas.78.7.4133. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Marsh M., Bolzau E., Helenius A. Penetration of Semliki Forest virus from acidic prelysosomal vacuoles. Cell. 1983 Mar;32(3):931–940. doi: 10.1016/0092-8674(83)90078-8. [DOI] [PubMed] [Google Scholar]
- Mooney J. J., Dalrymple J. M., Alving C. R., Russell P. K. Interaction of Sindbis virus with liposomal model membranes. J Virol. 1975 Feb;15(2):225–231. doi: 10.1128/jvi.15.2.225-231.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Newman G. C., Huang C. Structural studies on phophatidylcholine-cholesterol mixed vesicles. Biochemistry. 1975 Jul 29;14(15):3363–3370. doi: 10.1021/bi00686a012. [DOI] [PubMed] [Google Scholar]
- Silberkang M., Havel C. M., Friend D. S., McCarthy B. J., Watson J. A. Isoprene synthesis in isolated embryonic Drosophila cells. I. Sterol-deficient eukaryotic cells. J Biol Chem. 1983 Jul 10;258(13):8503–8511. [PubMed] [Google Scholar]
- White J., Helenius A. pH-dependent fusion between the Semliki Forest virus membrane and liposomes. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3273–3277. doi: 10.1073/pnas.77.6.3273. [DOI] [PMC free article] [PubMed] [Google Scholar]
- White J., Kartenbeck J., Helenius A. Membrane fusion activity of influenza virus. EMBO J. 1982;1(2):217–222. doi: 10.1002/j.1460-2075.1982.tb01150.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- White J., Kielian M., Helenius A. Membrane fusion proteins of enveloped animal viruses. Q Rev Biophys. 1983 May;16(2):151–195. doi: 10.1017/s0033583500005072. [DOI] [PubMed] [Google Scholar]