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Virology1983; 131(2); 394-408; doi: 10.1016/0042-6822(83)90507-x

Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants.

Abstract: Human and animal (avian and equine) influenza A virus isolates of the H3 serotype exhibit marked differences in their ability to bind specific sialyloligosaccharide sequences that serve as cell surface receptor determinants (G. Rogers and J. Paulson, 1983, Virology 127, 361-373). Whereas human isolates of this subtype strongly agglutinate enzymatically modified human erythrocytes containing the terminal SA alpha 2,6Gal sequence, avian and equine isolates preferentially agglutinate erythrocytes bearing the SA alpha 2, 3Gal sequence. As shown in this report, a glycoprotein found in horse serum, alpha 2-macroglobulin, is a potent inhibitor of viral adsorption to the cell surface for human H3 isolates. In contrast, avian and equine isolates are poorly inhibited suggesting a correlation between receptor specificity and inhibitor sensitivity. Growth of a human H3 isolate (A/Memphis/102/72) on MDCK cells in the presence of horse serum resulted in an overall shift in the virus receptor specificity from preferential binding of the SA alpha 2,6Gal linkage to preferential binding of the SA alpha 2,3Gal linkage characteristic of avian and equine isolates. Clonally isolated variants of A/Memphis/102/72 grown in the presence or absence of horse serum exhibited binding properties that account for those observed in the field isolates. Clones which preferentially bound the SA alpha 2,6Gal linkage, like the parent human virus, were very sensitive to inhibition of hemagglutination by horse serum and equine alpha 2-macroglobulin. In contrast, receptor variants which preferentially bound the SA alpha 2,3Gal linkage, like the avian and equine isolate, were insensitive to such inhibitors. None of the variants was very sensitive to inhibition of hemagglutination by human alpha 2-macroglobulin. These results suggest that the presence, in vivo, of a glycoprotein inhibitor such as equine alpha 2-macroglobulin could suppress infection of influenza viruses bearing an H3 hemagglutinin with a SA alpha 2,6Gal specific, inhibitor sensitive phenotype, allowing growth to predominance of a virus which is SA alpha 2,3Gal specific and inhibitor insensitive as found in avian and equine isolates.
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Publication Date: 1983-12-01 PubMed ID: 6197808DOI: 10.1016/0042-6822(83)90507-xGoogle 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

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates the differences in flu virus strains from humans, birds, and horses, and their sensitivity to a glycoprotein inhibitor. Researchers found that a horse serum glycoprotein inhibitor could potentially suppress the human influenza virus while having little effect on avian and equine viruses.

Study Overview

The study largely revolves around understanding different abilities of the H3 serotype influenza A virus, isolated from humans, birds, and horses, to bind with sialyloligosaccharide sequences on cell surfaces. These sequences play a role in the virus’s ability to infect cells. The nature of these sequences varies between different species, leading to the observed differences in the ability of different virus strains to bind them.

Experiment and Observations

  • While human-isolated viruses of H3 serotype strongly bind to cells containing specific sequences, avian and equine isolates prefer other specific sequences.
  • The researchers found that a glycoprotein in horse serum, alpha 2-macroglobulin, is a potent inhibitor of the virus’s ability to bind to the cell surface in instances of human isolates. Conversely, avian and equine isolates were less affected, suggesting a correlation between receptor specificity and sensitivity to the inhibitor.
  • When they grew a human H3 isolate on dog kidney cells (MDCK cells) in the presence of horse serum, they found that the virus’s receptor specificity shifted, showing a preference for the sequence favored by avian and equine isolates. This shift demonstrated the capacity for change under the influence of different environmental components.

Findings and Implications

  • The study also showed that different variants of the human H3 isolate that were grown with or without horse serum exhibited varying binding properties, reflecting the characteristics seen in human, avian, and equine isolates observed in the field. Variants that showed a preference for the sequence favored by the human virus were markedly sensitive to horse serum and the alpha 2-macroglobulin inhibitor. In contrast, variants favoring the sequence found in avian and equine viruses were generally resistant to such inhibitors.
  • These results led the researchers to speculate upon the potential role of a glycoprotein inhibitor such as equine alpha 2-macroglobulin in suppressing human influenza infection in vivo. A virus showing a preference for sequences found in avian and equine isolates and demonstrating resistance to the inhibitor could potentially grow to predominance.

The outcome of this research points to the potential use of glycoprotein inhibitors in controlling the spread of specific strains of the influenza virus in humans, offering possible directions for the development of new treatment strategies.

Cite This Article

APA
Rogers GN, Pritchett TJ, Lane JL, Paulson JC. (1983). Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants. Virology, 131(2), 394-408. https://doi.org/10.1016/0042-6822(83)90507-x

Publication

Virology
ISSN: 0042-6822
NlmUniqueID: 0110674
Country: United States
Language: English
Volume: 131
Issue: 2
Pages: 394-408

Researcher Affiliations

Rogers, G N
    Pritchett, T J
      Lane, J L
        Paulson, J C

          MeSH Terms

          • Adsorption
          • Animals
          • Chick Embryo
          • Ducks
          • Erythrocytes / immunology
          • Erythrocytes / microbiology
          • Glycoproteins / antagonists & inhibitors
          • Hemagglutination Inhibition Tests
          • Hemagglutination Tests
          • Hemagglutinins, Viral / analysis
          • Horses
          • Humans
          • Influenza A virus / drug effects
          • Receptors, Virus / drug effects
          • Viral Proteins / antagonists & inhibitors
          • alpha-Macroglobulins / pharmacology

          Grant Funding

          • AI-16165 / NIAID NIH HHS
          • GM07185 / NIGMS NIH HHS

          Citations

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