Binding of interferon to gangliosides

Besançon, Françoise; Ankel, Helmut

doi:10.1038/252478a0

Cited by 172 publications

(44 citation statements)

References 12 publications

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“…As components of the plasma membrane, they contribute to the carbohydrate-rich glycocalyx that determines the surface properties of cells (Ledeen & Yu, 1982). They have been implicated as physiological receptors for toxins (Bizzini et al, 1977;Cuatrecasas, 1973;Van Heyningen, 1974;Holmgren et al, 1975), hormones (Kohn et al, 1980), interferon (Cuatreeasas, 1973;Belardelli et al, 1982;Besancon & Ankel, 1974) (Yamakawa & Nagai, 1978). Some enveloped RNA viruses have been shown to bind to gangliosides that are effective as receptors (Haywood, 1974;Haywood & Boyer, 1981 ;Holmgren et al, 1980;Markwell et al, 1981Markwell et al, , 1984Bergelson et al, 1982;Umeda et aL, 1984;Suzuki et al, 1985).…”

Section: Introductionmentioning

confidence: 99%

Involvement of Gangliosides in Rabies Virus Infection

Superti

Hauttecoeur

Morelec

et al. 1986

Journal of General Virology

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SUMMARYThe role of gangliosides in rabies virus infection of chick embryo-related (CER) cells was investigated. Cultured cells were pretreated with neuraminidase to render the cells transiently non-susceptible to viral infection. Incubation of these desialylated cells with gangliosides allowed them to incorporate exogenous gangliosides and they recovered their susceptibility to rabies virus infection. Infection of CER cells was monitored by specific fluorescence 24 h after virus inoculation. The use of individual purified gangliosides or mixtures of two gangliosides to restore cellular susceptibility to viral infection showed that GTlb and GQlb were the most effective. The disialogangliosides were also active, principally GD 1 b, whereas GM 1, GM3 were poorly active and GD3 inactive. Incubation of rabies virus with gangliosides prior to virus infection reduced the percentage of infected cells. The results indicate that highly sialylated gangliosides are part of the cellular membrane receptor structure for the attachment of infective rabies virus. However, it is possible that other glycoconjugates such as glycoproteins or glycolipids also participate as components of a receptor structure for rabies virus.

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Section: Introductionmentioning

confidence: 99%

Involvement of Gangliosides in Rabies Virus Infection

Superti

Hauttecoeur

Morelec

et al. 1986

Journal of General Virology

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“…Thus, although there are similarities in the carbohydrate structures found on gangliosides and on glycoproteins with complex or hybrid-type N-linked oligosaccharides, productive interaction of IFN-a//j with target cells is independent of the presence of such N-linked oligosaccharides on membrane glycoproteins. Our finding has additional significance for the interaction of IFN-c(/P with target cells, because it indicates that the inhibition of activity of IFN-aIp by the lectins from P. wlgaris (PHA-E and PHA-L) [33,341 has an explanation unrelated to a shared N-linked complex-type oligosaccharides binding site.…”

Section: N-iicetvlglucosaminjiiiran~feruse I To Ifn-p Is Intactmentioning

confidence: 78%

Senstivity to alpha/beta-interferon is independent of N-linked complex-type oligosaccharides on cell-surface-membrane glycoproteins

Parker

Ankel

1985

Eur J Biochem

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The extent of involvement of carbohydrate structures in the mechanism of action of a and [j-interferon (IFN-a, IFN-P) is undefined. In this report we examine the role of complex-type N-linked oligosaccharides in the response to these interferons. The response of mouse leukemia L1210S cells, grown in the prcsence of swainsonine, an inhibitor of Golgi mannosidase I1 [Tulsiani, D. R. P., Harris, T. M. and Touster, 0. (1982) J . Bid. Clzern. 257, 7936-7939; Elbein A. D., Solf, R., Dorling, P. R. and Vosbeck, K. (1981) Proc. Nut1 Acud. Sci. USA 78, 7393-73971, to mouse IFN-a/& both with respect to antiviral and antigrowth effects, remains intact in spite of the total absence of complex-type N-linked oligosaccharides. Also, there is no difference in the response to human I F N -j of a parental Chinese hamster ovary cell line and a mutant lacking P-N-acetylglucosaminyltransferase 1 and therefore unable to synthesize complex-type N-linked oligosaccharides [Stanley, P., Callibot, V. and Siminovitch, L. (1975) CeIf 6, 121 -1281. These results are significant in permitting the conclusion that the carbohydratespecific binding of IFN-a and IFN-/3 to gangliosides cannot be due to a similarity of the ganglioside carbohydrate to that of a glycoprotein containing a complex-type N-liked oligosaccharide.Action of a-interferon (IFN-a) and /%interferon (IFN-fi) appears to be initiated at the surface of target cells. The nature of the interaction between the cell surface and these interferons, that results in a biological response, remains unclarified. Target cells have been shown to have saturable, high-affinity binding sites, which recognize both IFN-a and IFN-[j [l -81. Additional evidence suggests that high-affinity binding is due to an IFNalP-specific protein receptor on the cell surface [9 -1 I]. Other components of the plasma membrane, gangliosides, bind IFN-a and IFN-P 112 -141. In order to test whether the binding of IFN-a and IFN-p to gangliosides could be attributed to a similarity of carbohydrate structure between the gangliosides and a glycoprotein receptor for interferon, we have investigated the role of complex-type N-linked oligosaccharides in the interferon response. Our approach was to examine the activity of IFN-a/J on target cells which lack N-linked complex-typc oligosaccharides. We have used mouse L 1210s cells grown in the presence of swainsonine, an inhibitor of Golgi mannosidase 11 [I 5, 161, which are completely inhibited in the biosynthesis of this class of oligosaccharides, and a mutant Chinese hamster ovary cell line, which lacks N-acetylglucosaminyltransferase I, the enzyme essential for the synthesis of these oligosaccharides [37]. EXPERIMENTAL PROCEDURE Muter i u Is Ce/l lines und cell cullurcThe L1210 mouse leukemia cell line was clone S6 from Dr. Ion Gresser (Institut de Recherches Scientifiques sur le Cancer, Villejuif, France). This cell line was recloned in soft agar and a freshly isolated clone was used for all experiments. The L1210S cell line was maintained in culture by periodically res...

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“…Both contaminants were present in amounts of 10% or less as judged from the relative intensities of the spots. Ganglioside affinity columns were prepared as described (10). The procedure involved coupling of polylysine to CNBr-activated Sepharose (18), followed by the attachment of mixed bovine brain gangliosides with carbodiimide (19).…”

Section: Methodsmentioning

confidence: 99%

“…Its antiviral action is inhibited after preincubation of target L cells with certain plant lectins, such as the lectin from Phaeseolus vulgaris (9) or the nontoxic agglutinin from Abrus precatorius (unpublished observation) and after preincubation of the interferon itself with gangliosides (10,11). This type of interferon binds to carbohydrate constituents of the ganglioside molecules and can be eluted from affinity columns containing covalently bound gangliosides by solutions of N-acetylneuraminyllactose, the trisaccharide common to most gangliosides (12).…”

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confidence: 99%

Mouse fibroblast (type I) and immune (type II) interferons: pronounced differences in affinity for gangliosides and in antiviral and antigrowth effects on mouse leukemia L-1210R cells.

Ankel¹,

Krishnamurti²,

Besançon³

et al. 1980

Proc. Natl. Acad. Sci. U.S.A.

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Different interferons can be obtained from the same animal species depending on the cells and (or) the inducers used. Interferons of type I and type II differ not only antigenically but also in molecular weight and stability at low pH. We have investigated whether mouse type I and type II interferons also differ in properties relating to their biological action. We present evidence which suggests that the molecular mechanism leading to antiviral and antiowth effects induced by both types of interferon in susceptible cells must differ in at least one important step. Antiviral and antigrowth activities of type I but not of type II interferon are both inhibited when gangliosides are added to cell cultures together with the interferon. Whereas type I interferon strongly binds to ganglioside affinity columns and can be eluted with solutions of N-acetylneuraminyllactose, type II interferon passes through such columns unretarded.

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Binding of interferon to gangliosides

Cited by 172 publications

References 12 publications

Involvement of Gangliosides in Rabies Virus Infection

Involvement of Gangliosides in Rabies Virus Infection

Senstivity to alpha/beta-interferon is independent of N-linked complex-type oligosaccharides on cell-surface-membrane glycoproteins

Mouse fibroblast (type I) and immune (type II) interferons: pronounced differences in affinity for gangliosides and in antiviral and antigrowth effects on mouse leukemia L-1210R cells.

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