Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus
A purified sulfated xylomannan, named F6, obtained from the red seaweed Nothogenia fastigiata, proved to be a potent inhibitor of HSV-1 in vitro without affecting cell viability. In a virus yield reduction assay, the inhibitory concentration 50% (IC50) was 0.66 μg/ml. The mode of action of F6 was as...
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1998
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09447113_v5_n3_p205_Pujol http://hdl.handle.net/20.500.12110/paper_09447113_v5_n3_p205_Pujol |
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paper:paper_09447113_v5_n3_p205_Pujol2023-06-08T15:53:49Z Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus Pujol, Carlos Alberto Matulewicz, María Cristina Cerezo, Alberto Saúl Damonte, Elsa Beatriz Glycoprotein Hemagglutination inhibition Herpes simplex virus Natural antiviral Rosette inhibition Sulfated polysaccharide algae Herpes Human herpesvirus 1 Nothogenia fastigiata Ovis aries Simplexvirus A purified sulfated xylomannan, named F6, obtained from the red seaweed Nothogenia fastigiata, proved to be a potent inhibitor of HSV-1 in vitro without affecting cell viability. In a virus yield reduction assay, the inhibitory concentration 50% (IC50) was 0.66 μg/ml. The mode of action of F6 was ascribed to an inhibitory effect on virus adsorption. The glycoprotein C (gC) of HSV-1 is involved in virus binding to the cell surface heparan sulfate. Furthermore, it mediates other biological activities such as induction of hemagglutination and binding to the third component of complement C3b. The compound F6 was effective in inhibiting hemagglutination induced by HSV-1 and also causes a reduction of 50% in rosette formation between sheep red blood cells coupled to C3b and cells infected with HSV-1, when added to the reaction mixture in a final concentration of 0.39 and 0.90 μg/ml, respectively. These experiments demonstrate that F6 not only inhibits the adsorption of HSV-1 to susceptible cells but also interferes with other biological properties of the virus in which gC is involved, supporting the hypothesis of an interaction between F6 and the viral glycoprotein. Fil:Pujol, C.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Matulewicz, M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cerezo, A.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Damonte, E.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09447113_v5_n3_p205_Pujol http://hdl.handle.net/20.500.12110/paper_09447113_v5_n3_p205_Pujol |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Glycoprotein Hemagglutination inhibition Herpes simplex virus Natural antiviral Rosette inhibition Sulfated polysaccharide algae Herpes Human herpesvirus 1 Nothogenia fastigiata Ovis aries Simplexvirus |
spellingShingle |
Glycoprotein Hemagglutination inhibition Herpes simplex virus Natural antiviral Rosette inhibition Sulfated polysaccharide algae Herpes Human herpesvirus 1 Nothogenia fastigiata Ovis aries Simplexvirus Pujol, Carlos Alberto Matulewicz, María Cristina Cerezo, Alberto Saúl Damonte, Elsa Beatriz Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
topic_facet |
Glycoprotein Hemagglutination inhibition Herpes simplex virus Natural antiviral Rosette inhibition Sulfated polysaccharide algae Herpes Human herpesvirus 1 Nothogenia fastigiata Ovis aries Simplexvirus |
description |
A purified sulfated xylomannan, named F6, obtained from the red seaweed Nothogenia fastigiata, proved to be a potent inhibitor of HSV-1 in vitro without affecting cell viability. In a virus yield reduction assay, the inhibitory concentration 50% (IC50) was 0.66 μg/ml. The mode of action of F6 was ascribed to an inhibitory effect on virus adsorption. The glycoprotein C (gC) of HSV-1 is involved in virus binding to the cell surface heparan sulfate. Furthermore, it mediates other biological activities such as induction of hemagglutination and binding to the third component of complement C3b. The compound F6 was effective in inhibiting hemagglutination induced by HSV-1 and also causes a reduction of 50% in rosette formation between sheep red blood cells coupled to C3b and cells infected with HSV-1, when added to the reaction mixture in a final concentration of 0.39 and 0.90 μg/ml, respectively. These experiments demonstrate that F6 not only inhibits the adsorption of HSV-1 to susceptible cells but also interferes with other biological properties of the virus in which gC is involved, supporting the hypothesis of an interaction between F6 and the viral glycoprotein. |
author |
Pujol, Carlos Alberto Matulewicz, María Cristina Cerezo, Alberto Saúl Damonte, Elsa Beatriz |
author_facet |
Pujol, Carlos Alberto Matulewicz, María Cristina Cerezo, Alberto Saúl Damonte, Elsa Beatriz |
author_sort |
Pujol, Carlos Alberto |
title |
Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
title_short |
Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
title_full |
Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
title_fullStr |
Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
title_full_unstemmed |
Inhibitory action of an algal derived xylomannan on glycoprotein C - Mediated biological properties of Herpes simplex virus |
title_sort |
inhibitory action of an algal derived xylomannan on glycoprotein c - mediated biological properties of herpes simplex virus |
publishDate |
1998 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09447113_v5_n3_p205_Pujol http://hdl.handle.net/20.500.12110/paper_09447113_v5_n3_p205_Pujol |
work_keys_str_mv |
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1768542465785069568 |