ArticleJournal of virology1999
The hemagglutinin-esterase of mouse hepatitis virus strain S is a sialate-4-O-acetylesterase.
Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 72 citations in OpenAlex.
- Development and applications of sialoglycan-recognizing probes (SGRPs) with defined specificities: exploring the dynamic mammalian sialoglycome.Glycobiology · 2022Article
- Destruction of the vascular viral receptor in infectious salmon anaemia provides in vivo evidence of homologous attachment interference.PLoS pathogens · 2022Article
- Mucin Transiently Sustains Coronavirus Infectivity through Heterogenous Changes in Phase Morphology of Evaporating Aerosol.Viruses · 2022Article
- Article
- Porcine Deltacoronavirus Utilizes Sialic Acid as an Attachment Receptor and Trypsin Can Influence the Binding Activity.Viruses · 2021Article
- SDAV, the Rat Coronavirus-How Much Do We Know about It in the Light of Potential Zoonoses.Viruses · 2021Review
- Sialic Acids as Receptors for Pathogens.Biomolecules · 2021Review
- Synthetic O-acetylated sialosides facilitate functional receptor identification for human respiratory viruses.Nature chemistry · 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
- 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
- Review
- Exploration of the Sialic Acid World.Advances in carbohydrate chemistry and biochemistry · 2018Review
- Biological roles of glycans.Glycobiology · 2017Review
- Effective one-pot multienzyme (OPME) synthesis of monotreme milk oligosaccharides and other sialosides containing 4-O-acetyl sialic acid.Organic & biomolecular chemistry · 2016Article
- Coronavirus receptor switch explained from the stereochemistry of protein-carbohydrate interactions and a single mutation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Functions and Biosynthesis of O-Acetylated Sialic Acids.Topics in current chemistry · 2015Review
- Sialic Acid Receptors of Viruses.Topics in current chemistry · 2015Review
- The acetyl-esterase activity of the hemagglutinin-esterase protein of human coronavirus OC43 strongly enhances the production of infectious virus.Journal of virology · 2013Article
- The murine coronavirus hemagglutinin-esterase receptor-binding site: a major shift in ligand specificity through modest changes in architecture.PLoS pathogens · 2012Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By comparative analysis of the hemagglutinin-esterase (HE) protein of mouse hepatitis virus strain S (MHV-S) and the HE protein of influenza C virus, we found major differences in substrate specificities. In striking contrast to the influenza C virus enzyme, the MHV-S esterase was unable to release acetate from bovine submandibulary gland mucin. Furthermore, MHV-S could not remove influenza C virus receptors from erythrocytes. Analysis with free sialic acid derivatives revealed that the MHV-S HE protein specifically de-O-acetylates 5-N-acetyl-4-O-acetyl sialic acid (Neu4, 5Ac2) but not 5-N-acetyl-9-O-acetyl sialic acid (Neu5,9Ac2), which is the major substrate for esterases of influenza C virus and bovine coronaviruses. In addition, the MHV-S esterase converted glycosidically bound Neu4,5Ac2 of guinea pig serum glycoproteins to Neu5Ac. By expression of the MHV esterase with recombinant vaccinia virus and incubation with guinea pig serum, we demonstrated that the viral HE possesses sialate-4-O-acetylesterase activity. In addition to observed enzymatic activity, MHV-S exhibited affinity to guinea pig and horse serum glycoproteins. Binding required sialate-4-O-acetyl groups and was abolished by chemical de-O-acetylation. Since Neu4,5Ac2 has not been identified in mice, the nature of potential substrates and/or secondary receptors for MHV-S in the natural host remains to be determined. The esterase of MHV-S is the first example of a viral enzyme with high specificity and affinity toward 4-O-acetylated sialic acids.
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