SrasV1, PascalFrancis, Corpus, bibRecord, 000354

Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture

Identifieur interne : 000354 ( PascalFrancis/Corpus ); précédent : 000353; suivant : 000355

Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture

Auteurs : F. J. U. M. Van Der Meer ; C. A. M. De Haan ; N. M. P. Schuurman ; B. J. Haijema ; W. J. Peumans ; E. J. M. Van Damme ; P. L. Delputte ; J. Balzarini ; H. F. Egberink

Source :

Antiviral research [ 0166-3542 ] ; 2007.

RBID : Pascal:07-0413054

Descripteurs français

Pascal (Inist)
- Antiviral, Lectine, Nidovirales, In vitro, Culture cellulaire, Glycosylation, Luciferase, Essai, Technique immunoperoxydase, Activité biologique, Technique MTT.

English descriptors

KwdEn :
- Antiviral, Biological activity, Cell culture, Glycosylation, Immunoperoxidase technique, In vitro, Lectin, Luciferase, Nidovirales, Test.

Abstract

Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong to the order Nidovirales. So far antivirals are hardly available to combat infections with viruses of this order. Therefore, various antiviral strategies to counter nidoviral infections are under evaluation. Lectins, which bind to N-linked oligosaccharide elements of enveloped viruses, can be considered as a conceptionally new class of virus inhibitors. These agents were recently evaluated for their antiviral activity towards a variety of enveloped viruses and were shown in most cases to inhibit virus infection at low concentrations. However, limited knowledge is available for their efficacy towards nidoviruses. In this article the application of the plant lectins Hippeastrum hybrid agglutinin (HHA), Galanthus nivalis agglutinin (GNA), Cymbidium sp. agglutinin (CA) and Urtica dioica agglutinin (UDA) as well as non-plant derived pradimicin-A (PRM-A) and cyanovirin-N (CV-N) as potential antiviral agents was evaluated. Three antiviral tests were compared based on different evaluation principles: cell viability (MTT-based colorimetric assay), number of infected cells (immunoperoxidase assay) and amount of viral protein expression (luciferase-based assay). The presence of carbohydrate-binding agents strongly inhibited coronaviruses (transmissible gastroenteritis virus, infectious bronchitis virus, feline coronaviruses serotypes I and II, mouse hepatitis virus), arteriviruses (equine arteritis virus and porcine respiratory and reproductive syndrome virus) and torovirus (equine Berne virus). Remarkably, serotype II feline coronaviruses and arteriviruses were not inhibited by PRM-A, in contrast to the other viruses tested.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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Format Inist (serveur)

NO :	PASCAL 07-0413054 INIST
ET :	Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture
AU :	VAN DER MEER (F. J. U. M.); DE HAAN (C. A. M.); SCHUURMAN (N. M. P.); HAIJEMA (B. J.); PEUMANS (W. J.); VAN DAMME (E. J. M.); DELPUTTE (P. L.); BALZARINI (J.); EGBERINK (H. F.)
AF :	Department of Immunology and Infectious Diseases, Division of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1/3584 CL Utrecht/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 9 aut.); Department of Molecular Biology, UGent/Gent/Belgique (5 aut., 6 aut.); Laboratory of Virology, Department of Virology, Parasitology and Immunology, Faculty of Veterinary Medicine, UGent/Merelbeke/Belgique (7 aut.); Rega Institute for Medical Research, K. U. Leuven, Minderbroedersstraat 10/3000 Leuven/Belgique (8 aut.)
DT :	Publication en série; Niveau analytique
SO :	Antiviral research; ISSN 0166-3542; Coden ARSRDR; Pays-Bas; Da. 2007; Vol. 76; No. 1; Pp. 21-29; Bibl. 1 p.3/4
LA :	Anglais
EA :	Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong to the order Nidovirales. So far antivirals are hardly available to combat infections with viruses of this order. Therefore, various antiviral strategies to counter nidoviral infections are under evaluation. Lectins, which bind to N-linked oligosaccharide elements of enveloped viruses, can be considered as a conceptionally new class of virus inhibitors. These agents were recently evaluated for their antiviral activity towards a variety of enveloped viruses and were shown in most cases to inhibit virus infection at low concentrations. However, limited knowledge is available for their efficacy towards nidoviruses. In this article the application of the plant lectins Hippeastrum hybrid agglutinin (HHA), Galanthus nivalis agglutinin (GNA), Cymbidium sp. agglutinin (CA) and Urtica dioica agglutinin (UDA) as well as non-plant derived pradimicin-A (PRM-A) and cyanovirin-N (CV-N) as potential antiviral agents was evaluated. Three antiviral tests were compared based on different evaluation principles: cell viability (MTT-based colorimetric assay), number of infected cells (immunoperoxidase assay) and amount of viral protein expression (luciferase-based assay). The presence of carbohydrate-binding agents strongly inhibited coronaviruses (transmissible gastroenteritis virus, infectious bronchitis virus, feline coronaviruses serotypes I and II, mouse hepatitis virus), arteriviruses (equine arteritis virus and porcine respiratory and reproductive syndrome virus) and torovirus (equine Berne virus). Remarkably, serotype II feline coronaviruses and arteriviruses were not inhibited by PRM-A, in contrast to the other viruses tested.
CC :	002B02S05
FD :	Antiviral; Lectine; Nidovirales; In vitro; Culture cellulaire; Glycosylation; Luciferase; Essai; Technique immunoperoxydase; Activité biologique; Technique MTT
FG :	Virus; Oxidoreductases; Enzyme
ED :	Antiviral; Lectin; Nidovirales; In vitro; Cell culture; Glycosylation; Luciferase; Test; Immunoperoxidase technique; Biological activity
EG :	Virus; Oxidoreductases; Enzyme
SD :	Antiviral; Lectina; Nidovirales; In vitro; Cultivo celular; Glicosilación; Luciferase; Ensayo; Técnica inmunoperoxidasa; Actividad biológica
LO :	INIST-18839.354000150052680030
ID :	07-0413054

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Pascal:07-0413054

Le document en format XML

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<term>Biological activity</term>
<term>Cell culture</term>
<term>Glycosylation</term>
<term>Immunoperoxidase technique</term>
<term>In vitro</term>
<term>Lectin</term>
<term>Luciferase</term>
<term>Nidovirales</term>
<term>Test</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Antiviral</term>
<term>Lectine</term>
<term>Nidovirales</term>
<term>In vitro</term>
<term>Culture cellulaire</term>
<term>Glycosylation</term>
<term>Luciferase</term>
<term>Essai</term>
<term>Technique immunoperoxydase</term>
<term>Activité biologique</term>
<term>Technique MTT</term>
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<front><div type="abstract" xml:lang="en">Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong to the order Nidovirales. So far antivirals are hardly available to combat infections with viruses of this order. Therefore, various antiviral strategies to counter nidoviral infections are under evaluation. Lectins, which bind to N-linked oligosaccharide elements of enveloped viruses, can be considered as a conceptionally new class of virus inhibitors. These agents were recently evaluated for their antiviral activity towards a variety of enveloped viruses and were shown in most cases to inhibit virus infection at low concentrations. However, limited knowledge is available for their efficacy towards nidoviruses. In this article the application of the plant lectins Hippeastrum hybrid agglutinin (HHA), Galanthus nivalis agglutinin (GNA), Cymbidium sp. agglutinin (CA) and Urtica dioica agglutinin (UDA) as well as non-plant derived pradimicin-A (PRM-A) and cyanovirin-N (CV-N) as potential antiviral agents was evaluated. Three antiviral tests were compared based on different evaluation principles: cell viability (MTT-based colorimetric assay), number of infected cells (immunoperoxidase assay) and amount of viral protein expression (luciferase-based assay). The presence of carbohydrate-binding agents strongly inhibited coronaviruses (transmissible gastroenteritis virus, infectious bronchitis virus, feline coronaviruses serotypes I and II, mouse hepatitis virus), arteriviruses (equine arteritis virus and porcine respiratory and reproductive syndrome virus) and torovirus (equine Berne virus). Remarkably, serotype II feline coronaviruses and arteriviruses were not inhibited by PRM-A, in contrast to the other viruses tested.</div>
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<fA11 i1="01" i2="1"><s1>VAN DER MEER (F. J. U. M.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>DE HAAN (C. A. M.)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>SCHUURMAN (N. M. P.)</s1>
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<fA11 i1="04" i2="1"><s1>HAIJEMA (B. J.)</s1>
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<fA11 i1="05" i2="1"><s1>PEUMANS (W. J.)</s1>
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<fA11 i1="06" i2="1"><s1>VAN DAMME (E. J. M.)</s1>
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<fA11 i1="08" i2="1"><s1>BALZARINI (J.)</s1>
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<fA11 i1="09" i2="1"><s1>EGBERINK (H. F.)</s1>
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<fA14 i1="01"><s1>Department of Immunology and Infectious Diseases, Division of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1</s1>
<s2>3584 CL Utrecht</s2>
<s3>NLD</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>9 aut.</sZ>
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<fA14 i1="02"><s1>Department of Molecular Biology, UGent</s1>
<s2>Gent</s2>
<s3>BEL</s3>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
</fA14>
<fA14 i1="03"><s1>Laboratory of Virology, Department of Virology, Parasitology and Immunology, Faculty of Veterinary Medicine, UGent</s1>
<s2>Merelbeke</s2>
<s3>BEL</s3>
<sZ>7 aut.</sZ>
</fA14>
<fA14 i1="04"><s1>Rega Institute for Medical Research, K. U. Leuven, Minderbroedersstraat 10</s1>
<s2>3000 Leuven</s2>
<s3>BEL</s3>
<sZ>8 aut.</sZ>
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<fA20><s1>21-29</s1>
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<fA21><s1>2007</s1>
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<s5>354000150052680030</s5>
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<fC01 i1="01" l="ENG"><s0>Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong to the order Nidovirales. So far antivirals are hardly available to combat infections with viruses of this order. Therefore, various antiviral strategies to counter nidoviral infections are under evaluation. Lectins, which bind to N-linked oligosaccharide elements of enveloped viruses, can be considered as a conceptionally new class of virus inhibitors. These agents were recently evaluated for their antiviral activity towards a variety of enveloped viruses and were shown in most cases to inhibit virus infection at low concentrations. However, limited knowledge is available for their efficacy towards nidoviruses. In this article the application of the plant lectins Hippeastrum hybrid agglutinin (HHA), Galanthus nivalis agglutinin (GNA), Cymbidium sp. agglutinin (CA) and Urtica dioica agglutinin (UDA) as well as non-plant derived pradimicin-A (PRM-A) and cyanovirin-N (CV-N) as potential antiviral agents was evaluated. Three antiviral tests were compared based on different evaluation principles: cell viability (MTT-based colorimetric assay), number of infected cells (immunoperoxidase assay) and amount of viral protein expression (luciferase-based assay). The presence of carbohydrate-binding agents strongly inhibited coronaviruses (transmissible gastroenteritis virus, infectious bronchitis virus, feline coronaviruses serotypes I and II, mouse hepatitis virus), arteriviruses (equine arteritis virus and porcine respiratory and reproductive syndrome virus) and torovirus (equine Berne virus). Remarkably, serotype II feline coronaviruses and arteriviruses were not inhibited by PRM-A, in contrast to the other viruses tested.</s0>
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<fC02 i1="01" i2="X"><s0>002B02S05</s0>
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<s5>01</s5>
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<fC03 i1="01" i2="X" l="ENG"><s0>Antiviral</s0>
<s5>01</s5>
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<s5>02</s5>
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<s5>03</s5>
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<s2>NW</s2>
<s5>03</s5>
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<fC03 i1="03" i2="X" l="SPA"><s0>Nidovirales</s0>
<s2>NW</s2>
<s5>03</s5>
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<fC03 i1="04" i2="X" l="FRE"><s0>In vitro</s0>
<s5>04</s5>
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<s5>04</s5>
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<s5>04</s5>
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<s5>05</s5>
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<s5>05</s5>
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<s5>06</s5>
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<s5>06</s5>
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<s5>06</s5>
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<fC03 i1="07" i2="X" l="FRE"><s0>Luciferase</s0>
<s2>FE</s2>
<s5>07</s5>
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<fC03 i1="07" i2="X" l="ENG"><s0>Luciferase</s0>
<s2>FE</s2>
<s5>07</s5>
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<fC03 i1="07" i2="X" l="SPA"><s0>Luciferase</s0>
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<s5>08</s5>
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<s5>08</s5>
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<fC03 i1="09" i2="X" l="FRE"><s0>Technique immunoperoxydase</s0>
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<s5>10</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Actividad biológica</s0>
<s5>10</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Technique MTT</s0>
<s4>INC</s4>
<s5>86</s5>
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<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Virus</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Oxidoreductases</s0>
<s2>FE</s2>
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<fC07 i1="02" i2="X" l="ENG"><s0>Oxidoreductases</s0>
<s2>FE</s2>
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<s2>FE</s2>
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<s2>FE</s2>
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<fC07 i1="03" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="03" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
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<server><NO>PASCAL 07-0413054 INIST</NO>
<ET>Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture</ET>
<AU>VAN DER MEER (F. J. U. M.); DE HAAN (C. A. M.); SCHUURMAN (N. M. P.); HAIJEMA (B. J.); PEUMANS (W. J.); VAN DAMME (E. J. M.); DELPUTTE (P. L.); BALZARINI (J.); EGBERINK (H. F.)</AU>
<AF>Department of Immunology and Infectious Diseases, Division of Virology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1/3584 CL Utrecht/Pays-Bas (1 aut., 2 aut., 3 aut., 4 aut., 9 aut.); Department of Molecular Biology, UGent/Gent/Belgique (5 aut., 6 aut.); Laboratory of Virology, Department of Virology, Parasitology and Immunology, Faculty of Veterinary Medicine, UGent/Merelbeke/Belgique (7 aut.); Rega Institute for Medical Research, K. U. Leuven, Minderbroedersstraat 10/3000 Leuven/Belgique (8 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Antiviral research; ISSN 0166-3542; Coden ARSRDR; Pays-Bas; Da. 2007; Vol. 76; No. 1; Pp. 21-29; Bibl. 1 p.3/4</SO>
<LA>Anglais</LA>
<EA>Coronaviruses are important human and animal pathogens, the relevance of which increased due to the emergence of new human coronaviruses like SARS-CoV, HKU1 and NL63. Together with toroviruses, arteriviruses, and roniviruses the coronaviruses belong to the order Nidovirales. So far antivirals are hardly available to combat infections with viruses of this order. Therefore, various antiviral strategies to counter nidoviral infections are under evaluation. Lectins, which bind to N-linked oligosaccharide elements of enveloped viruses, can be considered as a conceptionally new class of virus inhibitors. These agents were recently evaluated for their antiviral activity towards a variety of enveloped viruses and were shown in most cases to inhibit virus infection at low concentrations. However, limited knowledge is available for their efficacy towards nidoviruses. In this article the application of the plant lectins Hippeastrum hybrid agglutinin (HHA), Galanthus nivalis agglutinin (GNA), Cymbidium sp. agglutinin (CA) and Urtica dioica agglutinin (UDA) as well as non-plant derived pradimicin-A (PRM-A) and cyanovirin-N (CV-N) as potential antiviral agents was evaluated. Three antiviral tests were compared based on different evaluation principles: cell viability (MTT-based colorimetric assay), number of infected cells (immunoperoxidase assay) and amount of viral protein expression (luciferase-based assay). The presence of carbohydrate-binding agents strongly inhibited coronaviruses (transmissible gastroenteritis virus, infectious bronchitis virus, feline coronaviruses serotypes I and II, mouse hepatitis virus), arteriviruses (equine arteritis virus and porcine respiratory and reproductive syndrome virus) and torovirus (equine Berne virus). Remarkably, serotype II feline coronaviruses and arteriviruses were not inhibited by PRM-A, in contrast to the other viruses tested.</EA>
<CC>002B02S05</CC>
<FD>Antiviral; Lectine; Nidovirales; In vitro; Culture cellulaire; Glycosylation; Luciferase; Essai; Technique immunoperoxydase; Activité biologique; Technique MTT</FD>
<FG>Virus; Oxidoreductases; Enzyme</FG>
<ED>Antiviral; Lectin; Nidovirales; In vitro; Cell culture; Glycosylation; Luciferase; Test; Immunoperoxidase technique; Biological activity</ED>
<EG>Virus; Oxidoreductases; Enzyme</EG>
<SD>Antiviral; Lectina; Nidovirales; In vitro; Cultivo celular; Glicosilación; Luciferase; Ensayo; Técnica inmunoperoxidasa; Actividad biológica</SD>
<LO>INIST-18839.354000150052680030</LO>
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Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture

Antiviral activity of carbohydrate-binding agents against Nidovirales in cell culture

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