Susceptibility of different strains of influenza a virus to the inhibitory effects of 2-deoxy-2,3-dehydro- N -trifluoroacetylneuraminic acid (FANA)
Identifieur interne : 002B72 ( Main/Exploration ); précédent : 002B71; suivant : 002B73Susceptibility of different strains of influenza a virus to the inhibitory effects of 2-deoxy-2,3-dehydro- N -trifluoroacetylneuraminic acid (FANA)
Auteurs : J. L. Schulman [États-Unis] ; P. Palese [États-Unis]Source :
- Virology [ 0042-6822 ] ; 1975.
English descriptors
- Teeft :
- Academic press, Assay, Biochemical differences, Cell culture, Clone cells, Different concentrations, Different strains, Fana, Fetuin, Hon2, Honl, Influenza, Influenza viruses, Inhibitor, Inhibitory, Inhibitory effects, Kilbourne, Neuraminidase, Neuraminidase activity, Neuraminidases, Palese, Plaque, Plaque assay, Recombinant, Recombinant strains, Recombinant viruses, Replication, Schulman, Susceptibility, Viral neuraminidases, Virus, Virus replication.
Abstract
Abstract: Susceptibility to the neuraminidase-inhibiting effects of a synthetic analog of neuraminic acid, 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA) was found to vary among different strains of influenza A virus according to the neuraminidase they contain. In particular, NWS (H0N1) virus and recombinant strains which derive their neuraminidase from NWS are especially susceptible to FANA as measured by the concentrations of inhibitor which reduce rates of elution from red cells, in vitro neuraminidase activity using fetuin as a substrate, and virus replication in cell culture under agar. Growth in tissue culture of X-7 (H0N2) virus and all recombinant viruses containing N2 neuraminidase is approximately 50–200 times less susceptible to inhibition by FANA. These results provide further evidence that the inhibitory effects of FANA on the replication of influenza viruses are mediated by its specific neuraminidase-inhibitory activity and confirm that neuraminidase activity is necessary for the replication of influenza viruses.
Url:
DOI: 10.1016/0042-6822(75)90374-8
Affiliations:
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L." last="Schulman">J. L. Schulman</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Department of Microbiology, Mount Sinai School of Medicine of the City University of New York, New York</wicri:cityArea></affiliation></author><author><name sortKey="Palese, P" sort="Palese, P" uniqKey="Palese P" first="P." last="Palese">P. Palese</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>Department of Microbiology, Mount Sinai School of Medicine of the City University of New York, New York</wicri:cityArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Virology</title><title level="j" type="abbrev">YVIRO</title><idno type="ISSN">0042-6822</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1975">1975</date><biblScope unit="volume">63</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="98">98</biblScope><biblScope unit="page" to="104">104</biblScope></imprint><idno type="ISSN">0042-6822</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0042-6822</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Assay</term><term>Biochemical differences</term><term>Cell culture</term><term>Clone cells</term><term>Different concentrations</term><term>Different strains</term><term>Fana</term><term>Fetuin</term><term>Hon2</term><term>Honl</term><term>Influenza</term><term>Influenza viruses</term><term>Inhibitor</term><term>Inhibitory</term><term>Inhibitory effects</term><term>Kilbourne</term><term>Neuraminidase</term><term>Neuraminidase activity</term><term>Neuraminidases</term><term>Palese</term><term>Plaque</term><term>Plaque assay</term><term>Recombinant</term><term>Recombinant strains</term><term>Recombinant viruses</term><term>Replication</term><term>Schulman</term><term>Susceptibility</term><term>Viral neuraminidases</term><term>Virus</term><term>Virus replication</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Susceptibility to the neuraminidase-inhibiting effects of a synthetic analog of neuraminic acid, 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA) was found to vary among different strains of influenza A virus according to the neuraminidase they contain. In particular, NWS (H0N1) virus and recombinant strains which derive their neuraminidase from NWS are especially susceptible to FANA as measured by the concentrations of inhibitor which reduce rates of elution from red cells, in vitro neuraminidase activity using fetuin as a substrate, and virus replication in cell culture under agar. Growth in tissue culture of X-7 (H0N2) virus and all recombinant viruses containing N2 neuraminidase is approximately 50–200 times less susceptible to inhibition by FANA. These results provide further evidence that the inhibitory effects of FANA on the replication of influenza viruses are mediated by its specific neuraminidase-inhibitory activity and confirm that neuraminidase activity is necessary for the replication of influenza viruses.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Schulman, J L" sort="Schulman, J L" uniqKey="Schulman J" first="J. L." last="Schulman">J. L. Schulman</name></region><name sortKey="Palese, P" sort="Palese, P" uniqKey="Palese P" first="P." last="Palese">P. Palese</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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