Receptor Specificity of Influenza A Viruses Correlates with the Agglutination of Erythrocytes from Different Animal Species
Identifieur interne : 000294 ( Istex/Curation ); précédent : 000293; suivant : 000295Receptor Specificity of Influenza A Viruses Correlates with the Agglutination of Erythrocytes from Different Animal Species
Auteurs : Toshihiro Ito [Japon] ; Yasuo Suzuki [Japon] ; Lyndon Mitnaul ; Angela Vines ; Hiroshi Kida [Japon] ; Yoshihiro KawaokaSource :
- Virology [ 0042-6822 ] ; 1997.
English descriptors
- Teeft :
- Academic press, Agglutinate, Agglutinate erythrocytes, Agglutinated, Animal species, Assay, Avian, Avian viruses, Chicken duck, Chicken erythrocytes, Different animal species, Direct binding assays, Equine, Equine erythrocytes, Equine viruses, Erythrocyte, Hemagglutinating activity, Hemagglutination, Horse erythrocytes, Human erythrocytes, Human transferrin, Human viruses, Influenza, Influenza viruses, Linkage, Maackia amurensis agglutinin, Microtiter, Microtiter assay, Microtiter plates, Neugc, Paulson, Receptor, Receptor specificities, Receptor specificity, Short communication table, Sialic, Sialic acid, Vira, Virology, Virus.
Abstract
Abstract: Despite their uniform ability to bind to oligosaccharide-containing terminal sialic acids, influenza A viruses show differences in receptor specificity. To test whether agglutination of erythrocytes from different animal species could be used to assess the receptor specificity of influenza A viruses, we determined the agglutinating activities of a range of virus strains, including those with known receptor specificities, using erythrocytes from seven animal species. All equine and avian viruses, including those known to recognizeN-acetyl andN-glycolyl sialic acid linked to galactose by the α2,3 linkage (NeuAcα2,3Gal and NeuGcα2,3Gal), agglutinated erythrocytes from all of the animal species tested (chickens, ducks, guinea pigs, humans, sheep, horses, and cows). The human viruses, including those known to preferentially recognize NeuAcα2,6Gal, agglutinated all but the horse and cow erythrocytes. Fluorescence-activated cell sorting analysis of erythrocytes using linkage-specific lectins [Sambucus nigraagglutinin for sialic acid (SA)α2,6Gal andMaackia amurensisagglutinin for SAα2,3Gal] showed that both cow and horse erythrocytes contain a large amount of SAα2,3Gal-, but virtually no SA2,6Gal-specific lectin-reactive oligosaccharides on the cell surface, while human and chicken erythrocytes contained both types of oligosaccharides. Considering that the majority (>93%) of sialic acid in horse and cow erythrocytes is of theN-glycolyl type, our results suggest that viruses able to agglutinate these erythrocytes (i.e., avian and equine viruses) recognize NeuGcα2,3Gal. These findings also show that agglutinating assays with erythrocytes from different animal species would be useful in characterizing the receptor specificity of influenza A viruses.
Url:
DOI: 10.1006/viro.1996.8323
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Lyndon Mitnaul<affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee, 38101-0318</mods:affiliation><wicri:noCountry code="subField">38101-0318</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee, 38101-0318</mods:affiliation><wicri:noCountry code="subField">38101-0318</wicri:noCountry></affiliation><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee, 38101-0318</mods:affiliation><wicri:noCountry code="subField">38101-0318</wicri:noCountry></affiliation>Le document en format XML
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Box 318, Memphis, Tennessee, 38101-0318</mods:affiliation><wicri:noCountry code="subField">38101-0318</wicri:noCountry></affiliation></author><author><name sortKey="Kida, Hiroshi" sort="Kida, Hiroshi" uniqKey="Kida H" first="Hiroshi" last="Kida">Hiroshi Kida</name><affiliation wicri:level="1"><mods:affiliation>Laboratory of Microbiology, Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, 060, Japan</mods:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Laboratory of Microbiology, Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, 060</wicri:regionArea></affiliation></author><author><name sortKey="Kawaoka, Yoshihiro" sort="Kawaoka, Yoshihiro" uniqKey="Kawaoka Y" first="Yoshihiro" last="Kawaoka">Yoshihiro Kawaoka</name><affiliation><mods:affiliation>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 332 N. Lauderdale, P.O. Box 318, Memphis, Tennessee, 38101-0318</mods:affiliation><wicri:noCountry code="subField">38101-0318</wicri:noCountry></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="1997">1997</date><biblScope unit="volume">227</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="493">493</biblScope><biblScope unit="page" to="499">499</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>Agglutinate</term><term>Agglutinate erythrocytes</term><term>Agglutinated</term><term>Animal species</term><term>Assay</term><term>Avian</term><term>Avian viruses</term><term>Chicken duck</term><term>Chicken erythrocytes</term><term>Different animal species</term><term>Direct binding assays</term><term>Equine</term><term>Equine erythrocytes</term><term>Equine viruses</term><term>Erythrocyte</term><term>Hemagglutinating activity</term><term>Hemagglutination</term><term>Horse erythrocytes</term><term>Human erythrocytes</term><term>Human transferrin</term><term>Human viruses</term><term>Influenza</term><term>Influenza viruses</term><term>Linkage</term><term>Maackia amurensis agglutinin</term><term>Microtiter</term><term>Microtiter assay</term><term>Microtiter plates</term><term>Neugc</term><term>Paulson</term><term>Receptor</term><term>Receptor specificities</term><term>Receptor specificity</term><term>Short communication table</term><term>Sialic</term><term>Sialic acid</term><term>Vira</term><term>Virology</term><term>Virus</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Despite their uniform ability to bind to oligosaccharide-containing terminal sialic acids, influenza A viruses show differences in receptor specificity. To test whether agglutination of erythrocytes from different animal species could be used to assess the receptor specificity of influenza A viruses, we determined the agglutinating activities of a range of virus strains, including those with known receptor specificities, using erythrocytes from seven animal species. All equine and avian viruses, including those known to recognizeN-acetyl andN-glycolyl sialic acid linked to galactose by the α2,3 linkage (NeuAcα2,3Gal and NeuGcα2,3Gal), agglutinated erythrocytes from all of the animal species tested (chickens, ducks, guinea pigs, humans, sheep, horses, and cows). The human viruses, including those known to preferentially recognize NeuAcα2,6Gal, agglutinated all but the horse and cow erythrocytes. Fluorescence-activated cell sorting analysis of erythrocytes using linkage-specific lectins [Sambucus nigraagglutinin for sialic acid (SA)α2,6Gal andMaackia amurensisagglutinin for SAα2,3Gal] showed that both cow and horse erythrocytes contain a large amount of SAα2,3Gal-, but virtually no SA2,6Gal-specific lectin-reactive oligosaccharides on the cell surface, while human and chicken erythrocytes contained both types of oligosaccharides. Considering that the majority (>93%) of sialic acid in horse and cow erythrocytes is of theN-glycolyl type, our results suggest that viruses able to agglutinate these erythrocytes (i.e., avian and equine viruses) recognize NeuGcα2,3Gal. These findings also show that agglutinating assays with erythrocytes from different animal species would be useful in characterizing the receptor specificity of influenza A viruses.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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