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[Receptor sialylsugar chains as determinants of host range of influenza viruses].

Abstract: All types of the hemagglutinin(HA) of human, pig, horse and aq. bird influenza A viruses, recognize sialyl lacto-series type I and II sugar chains(Sialic acid(SA) alpha 2-3(6)Gal beta 1-3(4) GlcNAc beta 1-) in glycoproteins and glycolipids in the target cells as common receptor molecules. Avian and equine influenza viruses preferentially binds the terminal sialic acid alpha 2-3Gal(SA2-3Gal) linkage, while human influenza viruses preferentially bind the SA2-6Gal linkage. SA distribution in animal species influence influenza virus host range. Swine trachea has both receptors for avian influenza viruses (SA2-3Gal specific) and for human influenza viruses(SA2-6Gal specific). In the case of horses, a virus with an HA recognizing Neu5Ac2-6Gal, but not Neu5Ac2-3Gal, failed to replicate in horses, while one with an HA recognizing the Neu5Gc2-3Gal moiety replicated in horses. The abundance of the Neu5Gc2-3Gal moiety in epithelial cells of horse trachea supports that recognition of Neu5Gc2-3Gal moiety is critical for viral replication in horses. The Neu5Gc2-3Gal is also associated with viral replication in duck intestine, primarily in the crypt epitherial cells. Such recognition, together with biochemical evidence of Neu5Gc in crypt cells, correlated exactly with the ability of the virus to replicate in duck colon. These results indicate the evidence of biologic effect of different sialic acid species in different animals.
Publication Date: 2001-02-28 PubMed ID: 11225305
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Summary

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The research explores how influenza A viruses, found in humans, pigs, horses, and aquatic birds, identify and bind to specific sugar chains on cell receptors based on the presence of different forms of sialic acid, which influences the range of hosts the virus can infect.

Understanding Virus Attack Mechanisms

  • The hemagglutinin (HA) found in influenza A viruses from diverse host species, recognizes specific sugar chains, known as sialyl lacto-series type I and II, in the target cells’ glycoproteins and glycolipids. This recognition serves as a common receptor molecule allowing the virus to infect different organisms.
  • The study points out that the distribution of sialic acid (SA) variations in different animal species can steer the host range that an influenza virus strain can infect.

Specificity of Virus Binding

  • The nature of binding is determined by the specificity of the virus for different SA linkages. Avian and equine influenza viruses preferentially bind to SA2-3Gal linkage, whereas human influenza viruses are attracted to the SA2-6Gal linkage.
  • The variety of receptors sets the proficiency of the virus to infect different hosts. As an example, swine trachea carries both receptors – for avian influenza viruses (SA2-3Gal specific) and for human influenza viruses (SA2-6Gal specific).

Implications for Viral Replication

  • In horses, an HA virus that recognizes Neu5Ac2-6Gal failed to replicate, implying that such a receptor binding site does not favor viral proliferation. However, another virus-HA that could recognize Neu5Gc2-3Gal was able to replicate, suggesting that this molecular interaction is pivotal for viral replication in horses.
  • The high prevalence of Neu5Gc2-3Gal in horse trachea epithelial cells lends support to this observation.

Sialic Acid Species and Viral Replication

  • Moreover, Neu5Gc2-3Gal also plays a role in viral replication in the duck intestine, primarily in the crypt epithelial cells. The ability of a virus to replicate in the duck’s colon coincided with the presence of Neu5Gc in crypt cells.
  • These findings underscore the biological effect of different sialic acid species in different animals, not only defining host range of influenza viruses but also influencing the virus’s ability to replicate within the host.

Cite This Article

APA
Suzuki Y. (2001). [Receptor sialylsugar chains as determinants of host range of influenza viruses]. Nihon Rinsho, 58(11), 2206-2210.

Publication

ISSN: 0047-1852
NlmUniqueID: 0420546
Country: Japan
Language: jpn
Volume: 58
Issue: 11
Pages: 2206-2210

Researcher Affiliations

Suzuki, Y
  • Department of Biochemistry, University of Shizuoka School of Pharmaceutical Sciences.

MeSH Terms

  • Animals
  • Glycolipids / analysis
  • Glycoproteins / analysis
  • Humans
  • Orthomyxoviridae / physiology
  • Receptors, Virus / chemistry
  • Sialic Acids / analysis

References

This article includes 14 references

Citations

This article has been cited 2 times.
  1. Branda F, Yon DK, Albanese M, Binetti E, Giovanetti M, Ciccozzi A, Ciccozzi M, Scarpa F, Ceccarelli G. Equine Influenza: Epidemiology, Pathogenesis, and Strategies for Prevention and Control. Viruses 2025 Feb 21;17(3).
    doi: 10.3390/v17030302pubmed: 40143233google scholar: lookup
  2. Singh RK, Dhama K, Karthik K, Khandia R, Munjal A, Khurana SK, Chakraborty S, Malik YS, Virmani N, Singh R, Tripathi BN, Munir M, van der Kolk JH. A Comprehensive Review on Equine Influenza Virus: Etiology, Epidemiology, Pathobiology, Advances in Developing Diagnostics, Vaccines, and Control Strategies. Front Microbiol 2018;9:1941.
    doi: 10.3389/fmicb.2018.01941pubmed: 30237788google scholar: lookup