Influenza C virus and bovine coronavirus esterase reveal a similar catalytic mechanism: new insights for drug discovery
Identifieur interne : 003969 ( Main/Exploration ); précédent : 003968; suivant : 003970Influenza C virus and bovine coronavirus esterase reveal a similar catalytic mechanism: new insights for drug discovery
Auteurs : Juliane Mayr [Autriche] ; Thomas Haselhorst [Australie] ; Martijn A. Langereis [Pays-Bas] ; Jeffrey C. Dyason [Australie] ; Wolfgang Huber [Autriche] ; Barbara Frey [Australie] ; Reinhard Vlasak [Autriche] ; Raoul J. De Groot [Pays-Bas] ; Mark Von Itzstein [Australie]Source :
- Glycoconjugate Journal [ 0282-0080 ] ; 2008-07-01.
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Abstract
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 α-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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DOI: 10.1007/s10719-007-9094-4
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Here we report nuclear magnetic resonance and molecular modelling studies on the 9-O-acetyl esterase showing that the α-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. 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