PMC:7029759 / 17743-19638 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":"There are two known options for agents to bind to ACE2. The first is using the small receptor-binding domain (RBD) from the SARS S protein that has been shown to be the key domain that binds the ACE2 receptor during entry 44. Administration of this domain, 193 amino acids in size, has been shown to effectively block the entry of SARS in cell culture 44. It is well within reason that SARS RBD could be given to patients, thereby binding their ACE2 proteins on target cells, preventing infection ( Figure 1). There is also the potential for the equivalent RBD of 2019-nCoV to be produced and used as a therapy as well. This strategy assumes SARS and 2019-nCoV share the same binding site on ACE2, which is highly likely given the similar ACE2 binding sites of SARS and NL63 coronavirus The small size of the therapy, similar in size in nanobody domains from camelid antibodies, would enhance the perfusion of the biologic into tissues to more effectively bind to viral entry receptors 45. In regards to the outbreak situation that is ongoing, the small protein facilitates the rapid production of the therapy in bacteria potentially, which would help production yields 19. Moreover, bacterial production would allow RBD proteins to be produced in a wide range of production facilities today in China, which already has numerous contract research organization operations 46. Alternatively, the RBD protein could be attached to an Fc fragment for extended circulation, which was done for an equivalent 212 amino acid domain from MERS. The MERS RBD-Fc fusion demonstrated the ability to block viral infection toward cell receptors, as well as to stimulate an immune response against that specific viral domain in mice 47. Of note, since the RBD-Fc fusion would bind to normal cells, one would want to eliminate cytotoxic Fc domain functions through mutations that eliminate Fc receptor binding 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