PMC:7278709 / 52387-53822 JSONTXT

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{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7278709","sourcedb":"PMC","sourceid":"7278709","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7278709","text":" The emphasis is also on binding, not catalysis. The method is not specifically concerned with catalytic amino acid residues involved in neurominidase action (nor any other activity of cleaving modifying the glycan to reduce virus binding, e.g. esterases, deacetylases). While evidence of neuraminidase activity in SARS-CoV-2 would be very important, the current evidence is that focus should be on sialic acid binding. This is because of lack of any strong evidence for such enzymic activities at the time of writing, and also because neuraminidase inhibitors approved as dugs, Oseltamivir (Tamiflu), and Zanamivir (Relenza) have been tested on SARS-CoV-2 in vitro and were not found effective [15]. It is nonetheless the binding of the appropriate glycans containing sialic acid that may still be important for SARS-CoV and SARS-CoV-2 infection in vivo, as it is for other viruses [16]. The fact that other viruses, including other coronaviruses, require that function, followed by any demonstration that SARS-CoV and SARS-CoV-2 still possess that function, would suggest that it could still be a target for pharmaceutical drug development, at least as a preventative. This argument is not unique in its general form. For example, Fantani and colleagues believe that the SARS-CoV-2 also uses sialic acids linked to host cell surface gangliosides to somehow facilitate host cell entry and so could represent a therepeutic target 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