PMC:7029759 / 31865-33636 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/7029759","sourcedb":"PMC","sourceid":"7029759","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7029759","text":"One potential limitation of the ACE2-Fc strategy is that the increase in levels of extracellular ACE2 could have unknown effects on the body, particularly when elevated for a prolonged time via Fc domain extended half-life. Small levels of extracellular ACE2 are already secreted by tissues, so the circulation of this extracellular domain would not be unprecedented 72. Moreover, recombinant ACE2 protein was well-tolerated by healthy patients in a phase I trial, and by patients with lung injury in a phase II trial, suggesting treating 2019-nCoV patients with ACE2-Fc will also tolerated. If investigators are still concerned, critical amino acid(s) for ACE2 peptidase activity could be mutated to abolish the native function of this sequence, while retaining high affinity binding for SARS and 2019-nCoV S protein. Indeed, this possibility was previously investigated in generating an ACE2 and IgG1 fusion protein, which showed that mutation of histidine residues at position 374 and 378 of the ACE2 extracellular domain abolished peptidase activity, but retained high affinity binding to SARS S protein 56. Of course, ACE2 peptidase mutation would eliminate the beneficial effects from the recombinant protein delivery of ACE2 in treating lung injury, so it is recommended that retaining ACE2 enzyme activity be pursued first. Another potential concern is that receptor binding via an antibody format could inadvertently direct 2019-nCoV toward infecting Fc receptor (CD16) positive cells, which has been shown in vitro for neutralizing antibodies in MERS 73. It’s unclear what clinical significance this would have, and to what extent this would happen in vivo. Ultimately, clinical trials will be needed to delineate any specific side effects of ACE2-Fc 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