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Journal of virology2022; 96(5); e0212021; doi: 10.1128/jvi.02120-21

N-Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses.

Abstract: Influenza A viruses (IAV) initiate infection by binding to glycans with terminal sialic acids on the cell surface. Hosts of IAV variably express two major forms of sialic acid, -acetylneuraminic acid (NeuAc) and -glycolylneuraminic acid (NeuGc). NeuGc is produced in most mammals, including horses and pigs, but is absent in humans, ferrets, and birds. The only known naturally occurring IAV that exclusively bind NeuGc are extinct highly pathogenic equine H7N7 viruses. We determined the crystal structure of a representative equine H7 hemagglutinin (HA) in complex with NeuGc and observed high similarity in the receptor-binding domain with an avian H7 HA. To determine the molecular basis for NeuAc and NeuGc specificity, we performed systematic mutational analyses, based on the structural insights, on two distant avian H7 HAs and an H15 HA. We found that the A135E mutation is key for binding α2,3-linked NeuGc but does not abolish NeuAc binding. The additional mutations S128T, I130V, T189A, and K193R converted the specificity from NeuAc to NeuGc. We investigated the residues at positions 128, 130, 135, 189, and 193 in a phylogenetic analysis of avian and equine H7 HAs. This analysis revealed a clear distinction between equine and avian residues. The highest variability was observed at key position 135, of which only the equine glutamic acid led to NeuGc binding. These results demonstrate that genetically distinct H7 and H15 HAs can be switched from NeuAc to NeuGc binding and vice versa after the introduction of several mutations, providing insights into the adaptation of H7 viruses to NeuGc receptors. Influenza A viruses cause millions of cases of severe illness and deaths annually. To initiate infection and replicate, the virus first needs to bind to a structure on the cell surface, like a key fitting in a lock. For influenza A viruses, these "keys" (receptors) on the cell surface are chains of sugar molecules (glycans). The terminal sugar on these glycans is often either -acetylneuraminic acid (NeuAc) or -glycolylneuraminic acid (NeuGc). Most influenza A viruses bind NeuAc, but a small minority bind NeuGc. NeuGc is present in species like horses, pigs, and mice but not in humans, ferrets, and birds. Here, we investigated the molecular determinants of NeuGc specificity and the origin of viruses that bind NeuGc.
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Publication Date: 2022-01-19 PubMed ID: 35044215PubMed Central: PMC8906439DOI: 10.1128/jvi.02120-21Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-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.

This research investigates how the Influenza A virus binds to chains of sugar molecules, particularly a type called N-glycolylneuraminic acid (NeuGc), to initiate infection in hosts. The study finds key mutations that allow the virus to bind with NeuGc, shedding light on the adaptation of Influenza A viruses to different hosts.

Introduction to Influenza A Virus

  • Influenza A Virus (IAV) causes severe illness and death each year across the globe.
  • To start an infection and replicate, the virus needs to connect to a structure on the cell surface—this mechanism is similar to a key fitting into a lock.

Understanding NeuAc and NeuGc Receptors

  • These “keys” or receptors on the cell surface are known as chains of sugar molecules (glycans). The terminal sugar on these glycans is either N-acetylneuraminic acid (NeuAc) or N-glycolylneuraminic acid (NeuGc).
  • While most IAVs bind to NeuAc, a small percentage binds to NeuGc.
  • NeuGc is found in different species such as horses, pigs, and mice, but it’s absent in humans, ferrets, and birds, creating distinctive avenues for the virus to infect different types of hosts.

Objectives of the Research

  • This study aims to investigate the molecular determinants of NeuGc specificity and the origin of viruses capable of binding to NeuGc.
  • By better understanding these mechanisms, researchers can further study the adaptation and evolution of the virus across species and develop new strategies for preventing and treating infections.

Findings of the Research

  • The researchers identified key mutations (A135E, S128T, I130V, T189A, and K193R) that switch the virus’s binding preference from NeuAc to NeuGc.
  • These results indicate that genetically distinct H7 and H15 influenza A viruses can change their binding specificity based on the introduction of certain mutations.
  • The highest variability was observed at the key position 135, where only the equine glutamic acid resulted in NeuGc binding. This reveals the significant role played by this specific amino acid in influencing the binding ability of the virus.
  • This knowledge provides valuable insight into how different influenza A strains adapt to recognize and bind with NeuGc receptors on host cells.

Cite This Article

APA
Spruit CM, Zhu X, Tomris I, Ríos-Carrasco M, Han AX, Broszeit F, van der Woude R, Bouwman KM, Luu MMT, Matsuno K, Sakoda Y, Russell CA, Wilson IA, Boons GJ, de Vries RP. (2022). N-Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses. J Virol, 96(5), e0212021. https://doi.org/10.1128/jvi.02120-21

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 96
Issue: 5
Pages: e0212021
PII: e02120-21

Researcher Affiliations

Spruit, Cindy M
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Zhu, Xueyong
  • Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Tomris, Ilhan
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Ríos-Carrasco, María
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Han, Alvin X
  • Department of Medical Microbiology, Amsterdam University Medical Center, Amsterdam, the Netherlands.
Broszeit, Frederik
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
van der Woude, Roosmarijn
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Bouwman, Kim M
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Luu, Michel M T
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
Matsuno, Keita
  • Division of Risk Analysis and Management, International Institute for Zoonosis Control, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
  • International Collaboration Unit, International Institute for Zoonosis Control, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
  • One Health Research Center, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
Sakoda, Yoshihiro
  • International Collaboration Unit, International Institute for Zoonosis Control, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
  • One Health Research Center, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
  • Laboratory of Microbiology, Department of Disease Control, Faculty of Veterinary Medicine, Hokkaido Universitygrid.39158.36, Sapporo, Japan.
Russell, Colin A
  • Department of Medical Microbiology, Amsterdam University Medical Center, Amsterdam, the Netherlands.
Wilson, Ian A
  • Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
  • Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA.
Boons, Geert-Jan
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.
  • Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia, USA.
de Vries, Robert P
  • Department of Chemical Biology & Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht Universitygrid.5477.1, Utrecht, the Netherlands.

MeSH Terms

  • Animals
  • Hemagglutinin Glycoproteins, Influenza Virus / chemistry
  • Hemagglutinin Glycoproteins, Influenza Virus / genetics
  • Hemagglutinin Glycoproteins, Influenza Virus / metabolism
  • Horses
  • Humans
  • Influenza A Virus, H7N7 Subtype / chemistry
  • Influenza A Virus, H7N7 Subtype / metabolism
  • N-Acetylneuraminic Acid
  • Neuraminic Acids / chemistry
  • Neuraminic Acids / metabolism
  • Phylogeny
  • Polysaccharides / metabolism
  • Protein Binding

Conflict of Interest Statement

The authors declare no conflict of interest.

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