ArticleProceedings of the National Academy of Sciences of the United States of America2009
Structural basis for ligand and substrate recognition by torovirus hemagglutinin esterases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 50 citations in OpenAlex.
- Evaluation of the Therapeutic Potential of Natural Peptides Against Hemagglutinin-Esterase of Bovine Coronavirus Based on Molecular Dynamics Simulation Studies.Veterinary medicine international · 2026Article
- Identification of a new goat torovirus strain: first detection and genomic analysis in China.Irish veterinary journal · 2025Article
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Article
- Review
- Sialic acid O-acetylation: From biosynthesis to roles in health and disease.The Journal of biological chemistry · 2021Review
- Development and use of a reverse transcription insulated isothermal PCR assay for detection and characterization of bovine torovirus in yaks.Archives of virology · 2021Article
- Recent Progress in Torovirus Molecular Biology.Viruses · 2021Review
- 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
- First detection and genomic characteristics of bovine torovirus in dairy calves in China.Archives of virology · 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
- Interaction of the Amino-Terminal Domain of the ISAV Fusion Protein with a Cognate Cell Receptor.Pathogens (Basel, Switzerland) · 2020Article
- Effects of Probiotics BaSC06 on Intestinal Digestion and Absorption, Antioxidant Capacity, Microbiota Composition, and Macrophage Polarization in Pigs for Fattening.Frontiers in veterinary science · 2020Article
- Sialoglycovirology of Lectins: Sialyl Glycan Binding of Enveloped and Non-enveloped Viruses.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Review
- 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
- Porcine Torovirus (PToV)-A Brief Review of Etiology, Diagnostic Assays and Current Epidemiology.Frontiers in veterinary science · 2019Review
- Structure of the infectious salmon anemia virus receptor complex illustrates a unique binding strategy for attachment.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Betacoronavirus Adaptation to Humans Involved Progressive Loss of Hemagglutinin-Esterase Lectin Activity.Cell host & microbe · 2017Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hemagglutinin esterases (HEs), closely related envelope glycoproteins in influenza C and corona- and toroviruses, mediate reversible attachment to O-acetylated sialic acids (Sias). They do so by acting both as lectins and as receptor-destroying enzymes, functions exerted by separate protein domains. HE divergence was accompanied by changes in quaternary structure and in receptor and substrate specificity. The selective forces underlying HE diversity and the molecular basis for Sia specificity are poorly understood. Here we present crystal structures of porcine and bovine torovirus HEs in complex with receptor analogs. Torovirus HEs form homodimers with sialate-O-acetylesterase domains almost identical to corresponding domains in orthomyxo- and coronavirus HEs, but with unique lectin sites. Structure-guided biochemical analysis of the esterase domains revealed that a functionally, but not structurally conserved arginine-Sia carboxylate interaction is critical for the binding and positioning of glycosidically bound Sias in the catalytic pocket. Although essential for efficient de-O-acetylation of Sias, this interaction is not required for catalysis nor does it affect substrate specificity. In fact, the distinct preference of the porcine torovirus enzyme for 9-mono- over 7,9-di-O-acetylated Sias can be explained from a single-residue difference with HEs of more promiscuous specificity. Apparently, esterase and lectin pockets coevolved; also the porcine torovirus HE receptor-binding site seems to have been designed to use 9-mono- and exclude di-O-acetylated Sias, possibly as an adaptation to replication in swine. Our findings shed light on HE evolution and provide fundamental insight into mechanisms of substrate binding, substrate recognition, and receptor selection in this important class of virion proteins.
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