Targeting the entry step of SARS-CoV-2: a promising therapeutic approach

doi:10.1038/s41392-020-0195-x

Comment

. 2020 Jun 17;5(1):98.

doi: 10.1038/s41392-020-0195-x.

Targeting the entry step of SARS-CoV-2: a promising therapeutic approach

Jing Li¹, Peng Zhan², Xinyong Liu³

Affiliations

¹ Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China.
² Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China. zhanpeng1982@sdu.edu.cn.
³ Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China. xinyongl@sdu.edu.cn.

PMID: 32555145
PMCID: PMC7298436
DOI: 10.1038/s41392-020-0195-x

Comment

Targeting the entry step of SARS-CoV-2: a promising therapeutic approach

Jing Li et al. Signal Transduct Target Ther. 2020.

. 2020 Jun 17;5(1):98.

doi: 10.1038/s41392-020-0195-x.

Authors

Jing Li¹, Peng Zhan², Xinyong Liu³

Affiliations

¹ Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China.
² Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China. zhanpeng1982@sdu.edu.cn.
³ Department of Medicinal Chemistry, Key Laboratory of Chemical Biology, Ministry of Education, School of Pharmaceutical Sciences, Shandong University, Ji'nan, 250012, China. xinyongl@sdu.edu.cn.

PMID: 32555145
PMCID: PMC7298436
DOI: 10.1038/s41392-020-0195-x

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Figures

**Fig. 1**
Entry of SARS-CoV-2 into host cells depends on ACE2 and TMPRSS2, and effective treatment strategies can prevent this process. For example, a Antibodies raised against SARS-S could cross-neutralize SARS-2-S. b Camostat mesylate inhibits TMPRSS2 and interferes with this process.

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Comment on

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor.
Hoffmann M, Kleine-Weber H, Schroeder S, Krüger N, Herrler T, Erichsen S, Schiergens TS, Herrler G, Wu NH, Nitsche A, Müller MA, Drosten C, Pöhlmann S. Hoffmann M, et al. Cell. 2020 Apr 16;181(2):271-280.e8. doi: 10.1016/j.cell.2020.02.052. Epub 2020 Mar 5. Cell. 2020. PMID: 32142651 Free PMC article.

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References

1. Hoffmann M, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:1–10. doi: 10.1016/j.cell.2020.02.052. - DOI - PMC - PubMed
1. Shang, J. et al. Structural basis of receptor recognition by SARS-CoV-2. Nature.10.1038/s41586-020-2179-y (2020). - PMC - PubMed
1. Li W, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003;426:450–454. doi: 10.1038/nature02145. - DOI - PMC - PubMed
1. Matsuyama S, et al. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J. Virol. 2010;84:12658–12664. doi: 10.1128/JVI.01542-10. - DOI - PMC - PubMed
1. Yan R, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020;367:1444–1448. doi: 10.1126/science.abb2762. - DOI - PMC - PubMed

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[1] Hoffmann M, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:1–10. doi: 10.1016/j.cell.2020.02.052. - DOI - PMC - PubMed

[2] Hoffmann M, et al. SARS-CoV-2 cell entry depends on ACE2 and TMPRSS2 and is blocked by a clinically proven protease inhibitor. Cell. 2020;181:1–10. doi: 10.1016/j.cell.2020.02.052. - DOI - PMC - PubMed

[3] Shang, J. et al. Structural basis of receptor recognition by SARS-CoV-2. Nature.10.1038/s41586-020-2179-y (2020). - PMC - PubMed

[4] Shang, J. et al. Structural basis of receptor recognition by SARS-CoV-2. Nature.10.1038/s41586-020-2179-y (2020). - PMC - PubMed

[5] Li W, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003;426:450–454. doi: 10.1038/nature02145. - DOI - PMC - PubMed

[6] Li W, et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature. 2003;426:450–454. doi: 10.1038/nature02145. - DOI - PMC - PubMed

[7] Matsuyama S, et al. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J. Virol. 2010;84:12658–12664. doi: 10.1128/JVI.01542-10. - DOI - PMC - PubMed

[8] Matsuyama S, et al. Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2. J. Virol. 2010;84:12658–12664. doi: 10.1128/JVI.01542-10. - DOI - PMC - PubMed

[9] Yan R, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020;367:1444–1448. doi: 10.1126/science.abb2762. - DOI - PMC - PubMed

[10] Yan R, et al. Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020;367:1444–1448. doi: 10.1126/science.abb2762. - DOI - PMC - PubMed

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Targeting the entry step of SARS-CoV-2: a promising therapeutic approach

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