PMC:7352545 / 26663-27890 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7352545","sourcedb":"PMC","sourceid":"7352545","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7352545","text":"HEF is indeed an ancient type of SA-O-acetylesterase. In contrast to A/B, the influenza C virus bears one spike with triple functions of HEF as a homotrimer [46]. Each HEF subunit bears two Neu5,9Ac2-binding sites and binds to the 9-O-acetyl group. In parallel, another modification of O-acetylation is found. Indeed, influenza C virus bears SA-O-acetylesterase [47], which converts 5-N-acetyl-9-O-NeuAc (Neu5,9Ac2) to 5-Neu5Ac. The 9-O-acetyl SA is a unique determinant for the influenza C virus receptor and Neu5,9Ac2 is crucial for receptor activity, but not Neu5Gc or Neu5Ac [48]. Neu5,9Ac2 is an essential determinant for influenza virus C type-specific host cell tropism. NAs cleave the α-ketosidic linkages to the D-Gal or GalNAc. SA-O-acetylesterases cleave different O-acetyl linkages (Figure 5). The OH-group of Tyr224 and the guanidino group of Arg236 interact with the CH3CO-carbonyl oxygen [49]. HEF SA-O-acetylesterase is found in several enveloped (+) ssRNA viruses of influenza C virus and also in certain CoVs and toroviruses [47]. The CoVs are different from the orthomyxoviruses, which hold a segmented (−) ssRNA genome and are instead evolutionary linked to the family Coronaviridae, order Nidovirales 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