ArticlePLoS pathogens2012
The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
43 citing papers in PubMed, 65 citations in OpenAlex.
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- Host Glycan-Lectin Interplay in SARS-CoV-2 Infection.International journal of molecular sciences · 2026Review
- A survey of bovine coronavirus infections in cattle with respiratory disease in Chiba Prefecture, Japan.The Journal of veterinary medical science · 2026Article
- Characteristics of an emerging canine respiratory coronavirus in China.The veterinary quarterly · 2025Article
- Virion motility of sialoglycan-cleaving respiratory viruses.Npj viruses · 2025Review
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- Prevalence and Evolutionary Characteristics of Bovine Coronavirus in China.Veterinary sciences · 2024Article
- Article
- First isolation of bovine coronavirus with a three-amino-acid deletion in the N gene causing severe respiratory and digestive disease in calve.Frontiers in microbiology · 2024Article
- Identification and Comparison of the Sialic Acid-Binding Domain Characteristics of Avian Coronavirus Infectious Bronchitis Virus Spike Protein.Journal of virology · 2023Article
- Virus diversity, wildlife-domestic animal circulation and potential zoonotic viruses of small mammals, pangolins and zoo animals.Nature communications · 2023Article
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Article
- The Glycan-Binding Trait of the Sarbecovirus Spike N-Terminal Domain Reveals an Evolutionary Footprint.Journal of virology · 2022Article
- The structure of Phocaeicola vulgatus sialic acid acetylesterase.Acta crystallographica. Section D, Structural biology · 2022Article
- Mucins Inhibit Coronavirus Infection in a Glycan-Dependent Manner.ACS central science · 2022Article
- Review
- SDAV, the Rat Coronavirus-How Much Do We Know about It in the Light of Potential Zoonoses.Viruses · 2021Review
- Clinical and molecular aspects of veterinary coronaviruses.Virus research · 2021Review
- Anti-SARS-CoV-2 Natural Products as Potentially Therapeutic Agents.Frontiers in pharmacology · 2021Review
Corrections and comments
- Erratum issuedHeesters, Balthasar [corrected to Heesters, Balthasar A]
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The hemagglutinin-esterases (HEs), envelope glycoproteins of corona-, toro- and orthomyxoviruses, mediate reversible virion attachment to O-acetylated sialic acids (O-Ac-Sias). They do so through concerted action of distinct receptor-binding ("lectin") and receptor-destroying sialate O-acetylesterase ("esterase") domains. Most HEs target 9-O-acetylated Sias. In one lineage of murine coronaviruses, however, HE esterase substrate and lectin ligand specificity changed dramatically as these viruses evolved to use 4-O-acetylated Sias instead. Here we present the crystal structure of the lectin domain of mouse hepatitis virus (MHV) strain S HE, resolved both in its native state and in complex with a receptor analogue. The data show that the shift from 9-O- to 4-O-Ac-Sia receptor usage primarily entailed a change in ligand binding topology and, surprisingly, only modest changes in receptor-binding site architecture. Our findings illustrate the ease with which viruses can change receptor-binding specificity with potential consequences for host-, organ and/or cell tropism, and for pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.