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  • Influenza C virus and bovine coronavirus esterase reveal a similar catalytic mechanism: New insights for drug discovery

    Author(s)
    Mayr, Juliane
    Haselhorst, Thomas
    Langereis, Martijn A
    Dyason, Jeffrey C
    Huber, Wolfgang
    Frey, Barbara
    Vlasak, Reinhard
    de Groot, Raoul J
    von Itzstein, Mark
    Griffith University Author(s)
    von Itzstein, Mark
    Haselhorst, Thomas E.
    Year published
    2008
    Metadata
    Show full item record
    Abstract
    Both, the influenza C (INF-C) virus haemagglutinin esterase fusion and bovine coronavirus (BCoV) haemagglutinin esterase surface glycoproteins exhibit a lectin binding capability and a receptor-destroying 9-O-acetyl esterase activity that recognise 9-O-acetyl-N-acetylneuraminic acid (Neu5,9Ac2)-containing glycans. Here we report nuclear magnetic resonance and molecular modelling studies on the 9-O-acetyl esterase showing that the a-configured Neu5,9Ac2 is strictly preferred by the INF-C and BCoV esterases. Interestingly, we have discovered that the INF-C esterase function releases acetate independently of the chemical nature ...
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    Both, the influenza C (INF-C) virus haemagglutinin esterase fusion and bovine coronavirus (BCoV) haemagglutinin esterase surface glycoproteins exhibit a lectin binding capability and a receptor-destroying 9-O-acetyl esterase activity that recognise 9-O-acetyl-N-acetylneuraminic acid (Neu5,9Ac2)-containing glycans. Here we report nuclear magnetic resonance and molecular modelling studies on the 9-O-acetyl esterase showing that the a-configured Neu5,9Ac2 is strictly preferred by the INF-C and BCoV esterases. Interestingly, we have discovered that the INF-C esterase function releases acetate independently of the chemical nature of the aglycon moiety, whereas subtle differences in substrate recognition were found for BCoV esterase. Analysis of the apo and complexed X-ray crystal structure of INF-C esterase revealed that binding of 9-O-acetylated N-acetylneuraminic acids is a dynamic process that involves conformational rearrangement of serine-57 in the esterase active site. This study provides valuable insights towards the design of drugs to combat INF-C virus and coronavirus infections causing outbreaks of upper respiratory infections and severe diarrhea in calves, respectively.
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    Journal Title
    Glycoconjugate Journal
    Volume
    25
    Issue
    5
    Publisher URI
    http://www.springer.com/life+sci/biochemistry+and+biophysics/journal/10719
    DOI
    https://doi.org/10.1007/s10719-007-9094-4
    Subject
    Biochemistry and cell biology
    Medical microbiology
    Neurosciences
    Publication URI
    http://hdl.handle.net/10072/20253
    Collection
    • Journal articles

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