Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human
Identifieur interne : 001780 ( Main/Exploration ); précédent : 001779; suivant : 001781Differences in Receptor Specificity between the Influenza Viruses of Duck, Chicken, and Human
Auteurs : A. S. Gambaryan [Russie] ; S. S. Yamnikova [Russie] ; D. K. Lvov [Russie] ; J. S. Robertson [Royaume-Uni] ; R. G. Webster [États-Unis] ; M. N. Matrosovich [Russie]Source :
- Molecular Biology [ 0026-8933 ] ; 2002-05-01.
English descriptors
- KwdEn :
Abstract
Abstract: The affinity of the duck, chicken, and human influenza viruses to the host cell sialosides was determined, and considerable distinctions between duck and chicken viruses were found. Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.
Url:
DOI: 10.1023/A:1016023700050
Affiliations:
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Webster</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, 38105-2794, Memphis, Tennessee</wicri:regionArea><placeName><region type="state">Tennessee</region></placeName></affiliation></author><author><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. N. 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Duck viruses bind to a wide range of sialosides, including the short-stem gangliosides. Most of the chicken viruses, like human ones, lose the ability to bind these gangliosides, which strictly correlates with the appearance of carbohydrate at position 158–160. The affinity of the chicken viruses to sialoglycoconjugates of chicken intestine as well as chicken, monkey, and human respiratory epithelial cells exceeds that of the duck viruses. The human influenza viruses have high affinity to the same cells but do not bind at all to the duck epithelial cell. This testifies to the absence of 6"-sialylgalactose residues from the duck cells, in contrast to chicken and monkey cells. The alteration of the receptor specificity of chicken viruses in comparison with duck ones results in the similarity of the patterns of accessible cells for chicken and human influenza viruses. This may be the cause of the appearance of the line of H9N2 viruses from Hong Kong live bird markets with receptor specificity similar to that of H3N2 human viruses, and of the ability of H5N1 and H9N2 chicken influenza viruses to infect humans.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li><li>Russie</li><li>États-Unis</li></country><region><li>District fédéral central</li><li>Tennessee</li></region><settlement><li>Moscou</li></settlement></list><tree><country name="Russie"><noRegion><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name></noRegion><name sortKey="Gambaryan, A S" sort="Gambaryan, A S" uniqKey="Gambaryan A" first="A. S." last="Gambaryan">A. S. Gambaryan</name><name sortKey="Lvov, D K" sort="Lvov, D K" uniqKey="Lvov D" first="D. K." last="Lvov">D. K. Lvov</name><name sortKey="Matrosovich, M N" sort="Matrosovich, M N" uniqKey="Matrosovich M" first="M. N." last="Matrosovich">M. 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