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Virology1994; 205(1); 17-23; doi: 10.1006/viro.1994.1615

Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates.

Abstract: The receptor specificity of 56 H2 and H3 influenza virus isolates from various animal species has been determined to test the relevance of receptor specificity to the ecology of influenza virus. The results show that the receptor specificity of both H2 and H3 isolates evaluated for sialic acid linkage specificity and inhibition of hemagglutination by horse serum correlates with the species of origin, as postulated earlier for H3 strains based on a limited survey of five human, three avian, and one equine strain. Elucidation of the amino acid sequence of several human H2 receptor variants and analysis of known sequences of H2 and H3 isolates revealed that receptor specificity varies in association with an amino acid change at residues 228 in addition to the change at residue 226 previously documented to affect receptor specificity of H3 but not H1 isolates. Residues 226 and 228 are leucine and serine in human isolates, which preferentially bind sialic acid alpha 2,6-galactose beta 1,4-N-acetyl glucosamine (SA alpha 2,6Gal), and glutamine and glycine in avian and equine isolates, which exhibit specificity for sialic acid alpha-2,3-galactose beta-1,3-N-acetyl galactosamine (SA alpha 2,3Gal). The results demonstrate that the correlation of receptor specificity and species of origin is maintained across both H2 and H3 influenza virus serotypes and provide compelling evidence that influenza virus hosts exert selective pressure to maintain the receptor specificity characteristics of strains isolated from that species.
Publication Date: 1994-11-15 PubMed ID: 7975212DOI: 10.1006/viro.1994.1615Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

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This research examines how the receptor specificity, which refers to the ability of a virus to attach to a host cell, of H2 and H3 influenza virus isolates differs among humans, birds, and horses. The researchers found that the receptor specificity varies depending on the species from which a strain is isolated and is influenced by an animal host’s selective pressure.

Relevance of Receptor Specificity in Influenza Virus Ecology

  • The study tested the receptor specificity of 56 H2 and H3 influenza virus isolates from various species. The research aimed to establish the relevance of receptor specificity concerning the ecology of the influenza virus.
  • The results indicated that the receptor specificity of both H2 and H3 isolates for sialic acid linkage specificity and inhibition of hemagglutination by horse serum aligns with the isolates’ species of origin.

Amino Acid Sequences and Receptor Specificity

  • The study delved into the amino acid sequence to highlight the receptor specificity variation associated with an amino acid change at residues 228, in addition to a previously documented change at residue 226 that affects H3, but not H1, isolates.
  • Thus, the amino acid sequence plays a critical role in determining a virus strain’s receptor specificity.

Correlation Between Receptor Specificity and Species of Origin

  • The study verified that the correlation between receptor specificity and the species of origin remains consistent across both H2 and H3 influenza virus serotypes.
  • Human isolates favor a specific kind of sialic acid bond, while avian and equine isolates prefer another type, which suggests that receptor specificity varies in accordance with the species of the host.

Species-Related Selective Pressure

  • The study offers substantial evidence that the host species of the influenza virus can exercise selective pressure to maintain the receptor specificity characteristics of isolated strains from the specific species.
  • This means that the animal hosts could have a significant impact on receptor specificity, driving viral evolution within their species.

Cite This Article

APA
Connor RJ, Kawaoka Y, Webster RG, Paulson JC. (1994). Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology, 205(1), 17-23. https://doi.org/10.1006/viro.1994.1615

Publication

ISSN: 0042-6822
NlmUniqueID: 0110674
Country: United States
Language: English
Volume: 205
Issue: 1
Pages: 17-23

Researcher Affiliations

Connor, R J
  • Department of Biological Chemistry, UCLA School of Medicine 90024-1737.
Kawaoka, Y
    Webster, R G
      Paulson, J C

        MeSH Terms

        • Amino Acid Sequence
        • Amino Acids / genetics
        • Animals
        • Carbohydrate Sequence
        • Chick Embryo
        • Hemagglutinin Glycoproteins, Influenza Virus
        • Hemagglutinins, Viral / genetics
        • Influenza A virus / metabolism
        • Molecular Sequence Data
        • Receptors, Virus / metabolism
        • Species Specificity
        • Viral Envelope Proteins / genetics

        Grant Funding

        • AI 29599 / NIAID NIH HHS
        • AI-08831 / NIAID NIH HHS
        • CA-21765 / NCI NIH HHS

        Citations

        This article has been cited 393 times.