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A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.

A potentially more promising strategy would be to create an antibody-like molecule that would bind to the coronavirus itself, rather than shielding cells from being infected. For this strategy, it is proposed to use a soluble version of the ACE2 receptor that would bind to the S protein of 2019-nCoV thereby neutralizing the virus ( Figure 1). Again, the research on the SARS virus suggests this strategy is potentially promising. Soluble ACE2 receptor was demonstrated to block the SARS virus from infecting cells in culture 42. The reported affinity of soluble ACE2 for the SARS S protein was 1.70 nM, which is comparable to the affinities of monoclonal antibodies 55; it is likely that 2019-nCoV has similar affinity for ACE2. In order to use ACE2 as a therapy to treat patients, it would be advisable to convert soluble ACE2 into an immunoadhesin format fused to an immunoglobulin Fc domain (ACE2-Fc), thereby extending the lifespan of the circulating molecule, while also recruiting effector functions of the immune system against the virus. While not tested in an animal model, a previous study demonstrated that an ACE2 extracellular domain fused to the human IgG1 domain (ACE2-NN-Ig) was effective in neutralizing SARS coronavirus in vitro, with a 50% inhibitory concentration of 2 nM 56. This study provides evidence then that ACE2-Fc could similarly inhibit 2019-nCoV in vitro and potentially in patients.