Unknown

Dataset Information

0

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


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 (Neu5,9Ac(2))-containing glycans. Here we report nuclear magnetic resonance and molecular modelling studies on the 9-O-acetyl esterase showing that the alpha-configured Neu5,9Ac(2) 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.

SUBMITTER: Mayr J 

PROVIDER: S-EPMC7088442 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC104150 | biostudies-literature
| S-EPMC249325 | biostudies-other
| S-EPMC7092896 | biostudies-literature
| S-EPMC7131372 | biostudies-literature
| S-EPMC2449365 | biostudies-literature
| EMPIAR-10390 | biostudies-other
| S-EPMC7168545 | biostudies-literature
| S-EPMC9607061 | biostudies-literature
| S-EPMC6983846 | biostudies-literature
| S-EPMC5095397 | biostudies-literature