Abstract
Sendai virus is able to induce the fusion of human erythrocytes. Bivalent cations or ATP are not essential for polyerythrocyte formation. High fusion indices were obtained when Sendai virus was added to cells incubated in the presence of both EDTA and iodoacetic acid. Human erythrocyte ghosts prepared by gradual hemolysis still retain the potential to undergo virus-induced fusion. Fusion of human red blood cells without the addition of viruses was obtained by incubation of erythrocytes at pH 10.5 in the presence of Ca++ (40 mM) or by addition of phospholipase C Clostridium perfringens preparations to cells previously agglutinated or polylysine.
Full Text
The Full Text of this article is available as a PDF (811.7 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Apostolov K., Poste G. Interaction of Sendai virus with human erythrocytes: a system for the study of membrane fusion. Microbios. 1972 Dec;6(24):247–261. [PubMed] [Google Scholar]
- BANGHAM A. D., DAWSON R. M. Electrokinetic requirements for the reaction between Cl. perfringens alpha-toxin (phospholipase C) and phospholipid substrates. Biochim Biophys Acta. 1962 May 7;59:103–115. doi: 10.1016/0006-3002(62)90701-1. [DOI] [PubMed] [Google Scholar]
- Baker R. F. Fusion of human red blood cell membranes. J Cell Biol. 1972 Apr;53(1):244–249. doi: 10.1083/jcb.53.1.244. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Burger S. P., Fujii T., Hanahan D. J. Stability of the bovine erythrocyte membrane. Release of enzymes and lipid components. Biochemistry. 1968 Oct;7(10):3682–3700. doi: 10.1021/bi00850a048. [DOI] [PubMed] [Google Scholar]
- Burt D. H., Green J. W. The sodium permeability of butanol-treated erythrocytes. The role of calcium. Biochim Biophys Acta. 1971 Jan 5;225(1):46–55. doi: 10.1016/0005-2736(71)90282-3. [DOI] [PubMed] [Google Scholar]
- Bächi T., Howe C. Fusion of erythrocytes by Sendai virus studied by electron microscopy. Proc Soc Exp Biol Med. 1972 Oct;141(1):141–149. doi: 10.3181/00379727-141-36733. [DOI] [PubMed] [Google Scholar]
- De Boer E., Loyter A. Formation of polynucleate avian erythrocytes by polylysine and phospholipase C. FEBS Lett. 1971 Jul 8;15(5):325–327. doi: 10.1016/0014-5793(71)80326-5. [DOI] [PubMed] [Google Scholar]
- EYLAR E. H., MADOFF M. A., BRODY O. V., ONCLEY J. L. The contribution of sialic acid to the surface charge of the erythrocyte. J Biol Chem. 1962 Jun;237:1992–2000. [PubMed] [Google Scholar]
- Frish A., Gazitt Y., Loyter A. Metabolically controlled hemolysis of chicken erythrocytes. Biochim Biophys Acta. 1973 Feb 16;291(3):690–700. doi: 10.1016/0005-2736(73)90474-4. [DOI] [PubMed] [Google Scholar]
- Harris J. R., Brown J. N. Fractionation of the avian erythrocyte: an ultrastructural study. J Ultrastruct Res. 1971 Jul;36(1):8–23. doi: 10.1016/s0022-5320(71)80085-0. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Marchesi S. L., Steers E., Marchesi V. T., Tillack T. W. Physical and chemical properties of a protein isolated from red cell membranes. Biochemistry. 1970 Jan 6;9(1):50–57. doi: 10.1021/bi00803a007. [DOI] [PubMed] [Google Scholar]
- Marikovsky Y., Danon D., Katchalsky A. Agglutination by polylysine of young and old red blood cells. Biochim Biophys Acta. 1966 Jul 27;124(1):154–159. [PubMed] [Google Scholar]
- OKADA Y. Analysis of giant polynuclear cell formation caused by HVJ virus from Ehrlich's ascites tumor cells. III. Relationship between cell condition and fusion reaction or cell degeneration reaction. Exp Cell Res. 1962 Feb;26:119–128. doi: 10.1016/0014-4827(62)90207-0. [DOI] [PubMed] [Google Scholar]
- OKADA Y., NISHIDA S., TADOKORO J. Correlation between the hemagglutination titer and the virus particle number of HVJ. Biken J. 1961 Sep;4:209–213. [PubMed] [Google Scholar]
- Okada Y. Factors in fusion of cells by HVJ. Curr Top Microbiol Immunol. 1969;48:102–128. doi: 10.1007/978-3-642-46163-7_5. [DOI] [PubMed] [Google Scholar]
- Poole A. R., Howell J. I., Lucy J. A. Lysolecithin and cell fusion. Nature. 1970 Aug 22;227(5260):810–814. doi: 10.1038/227810a0. [DOI] [PubMed] [Google Scholar]
- Poste G., Allison A. C. Membrane fusion reaction: a theory. J Theor Biol. 1971 Jul;32(1):165–184. doi: 10.1016/0022-5193(71)90144-5. [DOI] [PubMed] [Google Scholar]
- Sabban E., Laster Y., Loyter A. Resolution of the hemolytic and the hydrolytic activities of phospholipase-C preparation from Clostridium perfringens. Eur J Biochem. 1972 Jul 24;28(3):373–380. doi: 10.1111/j.1432-1033.1972.tb01923.x. [DOI] [PubMed] [Google Scholar]
- Stanley P. E., Williams S. G. Use of the liquid scintillation spectrometer for determining adenosine triphosphate by the luciferase enzyme. Anal Biochem. 1969 Jun;29(3):381–392. doi: 10.1016/0003-2697(69)90323-6. [DOI] [PubMed] [Google Scholar]
- Toister Z., Loyter A. The mechanism of cell fusion. II. Formation of chicken erythrocyte polykaryons. J Biol Chem. 1973 Jan 25;248(2):422–432. [PubMed] [Google Scholar]
- Toister Z., Loyter A. Virus induced fusion of chicken erythrocytes. Biochem Biophys Res Commun. 1970 Dec 24;41(6):1523–1530. doi: 10.1016/0006-291x(70)90560-7. [DOI] [PubMed] [Google Scholar]
- Yanovsky A., Loyter A. The mechanism of cell fusion. I. Energy requirements for virus-induced fusion of Ehrlich ascites tumor cells. J Biol Chem. 1972 Jun 25;247(12):4021–4028. [PubMed] [Google Scholar]