Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
Identifieur interne : 002032 ( Main/Exploration ); précédent : 002031; suivant : 002033Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
Auteurs : E. Nobusawa [Japon] ; T. Aoyama [Japon] ; H. Kato [Japon] ; Y. Suzuki [Japon] ; Y. Tateno [Japon] ; K. Nakajima [Japon]Source :
- Virology [ 0042-6822 ] ; 1991.
English descriptors
- Teeft :
- Academic press, Acid, Acid residues, Acid sequences, Amino, Amino acid, Amino acid numbera serotype, Amino acid residue, Amino acid residues, Amino acid sequence homology, Amino acid sequences, Amino acids, Amino terminus, Antigenic, Avian, Cdna, Cell surface, Coding regions, Determinant, Erythrocyte, Farris method, Haemagglutinin, Hemagglutinin, Hemagglutinin genes, Hemolysis, Homology, Influenza, Influenza virus, Influenza viruses, Kawaoka, Nobusawa, Nucleotide, Nucleotide sequences, Other hand, Paulson, Peptide, Phylogenetic, Phylogenetic tree, Receptor, Receptor binding, Receptor specificity, Residue, Right edge, Serotype, Serotypes, Sialic acid, Subunit, Virology, Virus, Virus strains.
Abstract
Abstract: We determined the sequences of 7 serotypes (H4, H6, H8, H9, H11, H12, and H13) of hemagglutinin (HA) genes, which have not been reported so far. The coding regions consisted of 1692 nucleotides in H4, 1698 in H6, 1695 in H8, 1680 in H9, 1695 in H11, 1692 in H12, and 1698 in H13, and specified 564, 566, 565, 560, 565, 564, and 566 amino acids, respectively. By comparison of amino acid sequences, 13 HA serotypes could be divided into two families, i.e., an H1 group (H1, H2, H5, H6, H8, H9, H11, H12, and H13) and an H3 group (H3, H4, H7, and H10). The relationship was essentially similar to that reported by Air from the comparison of 80 amino-terminal amino acid sequence of 12 HA serotypes (G.M. Air, 1981, Proc. Nat. Acad. Sci. USA 78, 7639–7643). Though a considerable amino acid sequence difference exists between certain HA serotypes, several amino acid residues in fusion peptides (HA21–11) and receptor-binding sites (HA198, −134, −138, −153, −183, and −195) were shown to be conserved among the 13 HA serotypes. Human H1 and avian H3, H4, H8, and H10 viruses preferentially bound NeuAcα2,3Gal sequences, whereas human H2 and H3 and avian H6 and H9 viruses bound NeuAcα2,6Gal sequences, although the amino acid residues at position 226 of human H2 and avian H6 and H9 serotype HAs are glutamine. These results show that the amino acid residue at position 226 is not necessarily a determinant of receptor specificity for all serotypes.
Url:
DOI: 10.1016/0042-6822(91)90588-3
Affiliations:
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The coding regions consisted of 1692 nucleotides in H4, 1698 in H6, 1695 in H8, 1680 in H9, 1695 in H11, 1692 in H12, and 1698 in H13, and specified 564, 566, 565, 560, 565, 564, and 566 amino acids, respectively. By comparison of amino acid sequences, 13 HA serotypes could be divided into two families, i.e., an H1 group (H1, H2, H5, H6, H8, H9, H11, H12, and H13) and an H3 group (H3, H4, H7, and H10). The relationship was essentially similar to that reported by Air from the comparison of 80 amino-terminal amino acid sequence of 12 HA serotypes (G.M. Air, 1981, Proc. Nat. Acad. Sci. USA 78, 7639–7643). Though a considerable amino acid sequence difference exists between certain HA serotypes, several amino acid residues in fusion peptides (HA21–11) and receptor-binding sites (HA198, −134, −138, −153, −183, and −195) were shown to be conserved among the 13 HA serotypes. Human H1 and avian H3, H4, H8, and H10 viruses preferentially bound NeuAcα2,3Gal sequences, whereas human H2 and H3 and avian H6 and H9 viruses bound NeuAcα2,6Gal sequences, although the amino acid residues at position 226 of human H2 and avian H6 and H9 serotype HAs are glutamine. These results show that the amino acid residue at position 226 is not necessarily a determinant of receptor specificity for all serotypes.</div></front></TEI><affiliations><list><country><li>Japon</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Nobusawa, E" sort="Nobusawa, E" uniqKey="Nobusawa E" first="E." last="Nobusawa">E. Nobusawa</name></region><name sortKey="Aoyama, T" sort="Aoyama, T" uniqKey="Aoyama T" first="T." last="Aoyama">T. Aoyama</name><name sortKey="Kato, H" sort="Kato, H" uniqKey="Kato H" first="H." last="Kato">H. Kato</name><name sortKey="Nakajima, K" sort="Nakajima, K" uniqKey="Nakajima K" first="K." last="Nakajima">K. Nakajima</name><name sortKey="Suzuki, Y" sort="Suzuki, Y" uniqKey="Suzuki Y" first="Y." last="Suzuki">Y. Suzuki</name><name sortKey="Tateno, Y" sort="Tateno, Y" uniqKey="Tateno Y" first="Y." last="Tateno">Y. Tateno</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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