Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
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. Natl. 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 (HA2(1-11)) and receptor-binding sites (HA1(98), -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 NeuAc alpha 2,3Gal sequences, whereas human H2 and H3 and avian H6 and H9 viruses bound NeuAc alpha 2,6Gal 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.
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Influenza haemagglutinin is the main target for influenza A virus vaccines and drugs, and can be genetically classified into two main subgroups: group 1 and group 2.
“Influenza haemagglutinin (HA) is the main target for influenza A virus vaccines and drugs, and can be genetically classified into two main subgroups: group 1 and group 2 (refs. 30,31).”
From Design of protein-binding proteins from the target structure alone (2022) · cites this paper as [31]
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Design of protein-binding proteins from the target structure alone
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- Authors
- Nobusawa, E., Aoyama, T., Kato, H., Suzuki, Y., Tateno, Y., & Nakajima, K.
- Affiliations
- Tokyo Metropolitan Institute of Public Health (JP)
- Institute of Medical Science, The University of Tokyo (JP)
- Shizuoka University (JP)
- National Institute of Genetics (JP)
- Corresponding author
- Nobusawa, E.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 1991-06
- Volume
- 182
- Issue
- 2
- Pages
- 475-485
- ISSN
- 0042-6822 (ISSN-L)
- OpenAlex
- W2032378111
- Cited by
- 471
- References
- 42
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 8 · 2023: 9 · 2022: 7 · 2021: 12 · 2020: 18 · 2019: 17 · 2018: 20 · 2017: 18 · 2016: 19 · 2015: 15 · 2014: 26 · 2013: 27 · 2012: 29
- FWCI
- 7.77
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Virology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education
- Topics
- Health Sciences › Medicine › Epidemiology › Influenza Virus Research Studies
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- influenza A virus, hemagglutinin, receptor binding sites, fusion peptide, avian influenza, human influenza
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Cloning, Molecular, Genes, Viral, Hemagglutinins, Viral, Membrane Proteins, Molecular Sequence Data, Influenza A virus, Phylogeny, Receptors, Virus, Serotyping, Oligonucleotide Probes, Viral Structural Proteins
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