Abstract
Membrane receptors for rubella virus (RV) in Vero cells were studied by means of two different approaches: (i) by enzyme treatment of the whole cell membrane and (ii) by testing the ability of isolated plasma membrane molecules to compete with cells for virus binding. The replication of RV was studied with both indirect immunofluorescence assay and molecular hybridization techniques. Phospholipases A2 and C digestion of cells greatly reduced the infectivity by the virus, pointing towards the involvement of lipid structures as receptor sites for RV. Furthermore, susceptibility of Vero cells to virus infection was also reduced after β-N-acetyl-d-glucosaminidase, α-glucosidase and β-galactosidase treatment, suggesting that carbohydrate residues may participate in a complex cellular receptor structure for RV. When the major membrane lipids were examined separately for their ability to inhibit viral infectivity, several phospholipids (phosphatidylserine, phosphatidylinositol, phosphatidylethanolamine, phosphatidylcholine, sphingomyelin) and glycolipids (gangliosides, lactosylceramide, cerebroside sulphate) showed a strong neutralizing activity, confirming the role of membrane lipid moiety in the cell surface receptor for RV.
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References
Aminoff D (1959) The determination of free sialic acid in the presence of the bound compound. Virology 7:355–357
Banatvala JE, Best JM (1984) Rubella. In: Brown F, Wilson G (eds) Topley and Wilson's principles of bacteriology, virology and immunology, vol 4. 7th edn. Edward Arnold, London, pp 271–302
Best JM, Banatvala JE (1987) Rubella. In: Zuckerman AJ, Banatvala JE, Pattison JR (eds) Principles and practice of clinical virology. John Wiley and Sons, New York, pp 315–353
Cremer NE, Oshiro LS, Weil LM, Lennette EH, Itabashi HH, Carnay L (1975) Isolation of rubella virus from brain in chronic progressive panencephalitis. J Gen Virol 29:143–151
Dubois M, Giles KA, Hamilton JK, Rebers PA, Smith F (1956) Colorimetric method for determination of sugars and related substances. Anal Chem 28:350–356
Gahmberg CG (1981) Membrane glycoproteins and glycolipids: structure, localization and function of the carbohydrate. In: Finean JB, Michell RH, (eds) New comprehensive biochemistry, vol 1. Elsevier, Amsterdam, pp 127–160
Gillespie D, Bresser J (1981) mRNA immobilization in NaI: quick blots. Biotechnologies 6:184–190
Green KY, Dorsett PH (1986) Rubella virus antigens: localization of epitopes involved in hemagglutination and neutralization by using monoclonal antibodies. J Virol 57:893–898
Herrmann KL (1979) Rubella virus. In: Lennette EH, Schmidt NJ (eds) Diagnostic procedures for viral, rickettsial and chlamidial infections, 5th edn. American Public Health Association, Washington D.C., pp 725–766
Ho-Terry L, Terry GM, Cohen A, Londesborough P (1986) Immunological characterization of the rubella El glycoprotein. Arch Virol 90:145–152
Hunt RC, Moore NF (1980) Carbohydrates in cell membranes. In: Blough HA, Tiffany JM (eds) Cell membranes and viral envelopes, vol 1. Academic Press, London, pp 277–329
Lonberg-Holm K, Philipson L (1974) Attachment of virions to host cells. Monogr Virol 9:24–49
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Mastromarino P, Cioè L, Rieti S, Orsi N (1989) Binding sites for rubella virus on erythrocyte membrane. Arch Virol 107:15–26
Nunoue T, Goya N (1977) Nuclear and cytoplasmic immunofluorescence in CSF cells from neonate with congenital rubella. Microbiol Immunol 21:731–741
Ogra PL, Ogra SS, Chiba Y, Dzierba JL (1975) Rubella virus infection in juvenile rheumatoid arthritis. Lancet I 1157–1162
Oker-Blom C, Veman I, Kääriäinen L, Petterson R (1983) Rubella virus 40 S genome RNA specifies a 24 S subgenomic mRNA that codes for a precursor to structural proteins. J Virol 9:403–408
Seganti L, Mastromarino P, Superti F, Sinibaldi L, Orsi N (1981) Receptors for BK virus on human erythrocytes. Acta Virol 25:177–181
Shen L, Ginsburg V (1968) Release of sugars from HeLA cells by trypsin. In: Manson LA (ed) Biological properties of the mammalian surface membrane. Wistar Institute Press, Philadelphia, pp 67–71
Thomas PS (1980) Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci USA 77:5201–5205
Waxham MN, Wolinsky JS (1985) A model of the structural organization of rubella virions. Rev Infect Dis [Suppl] 7:133–139
Waxham MN, Wolinsky JS (1985) Detailed immunologie analysis of the structural polypeptides of rubella virus using monoclonal antibodies. Virology 143:153–165
Woods WA, Johnson RT, Hostetler DD, Lepow ML, Robbins FC (1966) Immunofluorescent studies on rubella-infected tissue cultures and human tissues. J Immunol 96:253–262
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Mastromarino, P., Cioè, L., Rieti, S. et al. Role of membrane phospholipids and glycolipids in the Vero cell surface receptor for rubella virus. Med Microbiol Immunol 179, 105–114 (1990). https://doi.org/10.1007/BF00198531
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DOI: https://doi.org/10.1007/BF00198531