ArticleProceedings of the National Academy of Sciences of the United States of America2016
Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.
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Who cites it
30 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.
- The Role of Host Genetic Factors in Coronavirus Susceptibility: Review of Animal and Systematic Review of Human Literature.American journal of human genetics · 2020Pooled it
- A Review: Bovine Coronavirus Evolution, Molecular Epidemiology, and Genetic Variation.Viruses · 2026Review
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- Chemoenzymatic Synthesis ofTetrahedron · 2023Article
- Article
- A Deadly Embrace: Hemagglutination Mediated by SARS-CoV-2 Spike Protein at Its 22 N-Glycosylation Sites, Red Blood Cell Surface Sialoglycoproteins, and Antibody.International journal of molecular sciences · 2022Review
- SDAV, the Rat Coronavirus-How Much Do We Know about It in the Light of Potential Zoonoses.Viruses · 2021Review
- Second sialic acid-binding site of influenza A virus neuraminidase: binding receptors for efficient release.The FEBS journal · 2021Article
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- Recent Progress in Torovirus Molecular Biology.Viruses · 2021Review
- A Chemoenzymatic Synthon Strategy for SynthesizingThe Journal of organic chemistry · 2020Article
- Coronavirus hemagglutinin-esterase and spike proteins coevolve for functional balance and optimal virion avidity.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Host Receptors of Influenza Viruses and Coronaviruses-Molecular Mechanisms of Recognition.Vaccines · 2020Review
- Cryo-EM structure of coronavirus-HKU1 haemagglutinin esterase reveals architectural changes arising from prolonged circulation in humans.Nature communications · 2020Article
- SARS-CoV-2 Evolutionary Adaptation toward Host Entry and Recognition of Receptor O-Acetyl Sialylation in Virus-Host Interaction.International journal of molecular sciences · 2020Review
- Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Structural basis for human coronavirus attachment to sialic acid receptors.Nature structural & molecular biology · 2019Article
- Alterations in sialic-acid O-acetylation glycoforms during murine erythrocyte development.Glycobiology · 2019Article
- Human coronaviruses OC43 and HKU1 bind to 9-Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Virus recognition of glycan receptors.Current opinion in virology · 2019Review
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemagglutinin-esterases (HEs) are bimodular envelope proteins of orthomyxoviruses, toroviruses, and coronaviruses with a carbohydrate-binding "lectin" domain appended to a receptor-destroying sialate-O-acetylesterase ("esterase"). In concert, these domains facilitate dynamic virion attachment to cell-surface sialoglycans. Most HEs (type I) target 9-O-acetylated sialic acids (9-O-Ac-Sias), but one group of coronaviruses switched to using 4-O-Ac-Sias instead (type II). This specificity shift required quasisynchronous adaptations in the Sia-binding sites of both lectin and esterase domains. Previously, a partially disordered crystal structure of a type II HE revealed how the shift in lectin ligand specificity was achieved. How the switch in esterase substrate specificity was realized remained unresolved, however. Here, we present a complete structure of a type II HE with a receptor analog in the catalytic site and identify the mutations underlying the 9-O- to 4-O-Ac-Sia substrate switch. We show that (i) common principles pertaining to the stereochemistry of protein-carbohydrate interactions were at the core of the transition in lectin ligand and esterase substrate specificity; (ii) in consequence, the switch in O-Ac-Sia specificity could be readily accomplished via convergent intramolecular coevolution with only modest architectural changes in lectin and esterase domains; and (iii) a single, inconspicuous Ala-to-Ser substitution in the catalytic site was key to the emergence of the type II HEs. Our findings provide fundamental insights into how proteins "see" sugars and how this affects protein and virus evolution.
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