The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
Open accessAbstract
The severe acute respiratory syndrome (SARS) pandemic revealed that zoonotic transmission of animal coronaviruses (CoV) to humans poses a significant threat to public health and warrants surveillance and the development of countermeasures. The activity of host cell proteases, which cleave and activate the SARS-CoV spike (S) protein, is essential for viral infectivity and constitutes a target for intervention. However, the identities of the proteases involved have been unclear. Pioneer studies identified cathepsins and type II transmembrane serine proteases as cellular activators of SARS-CoV and demonstrated that several emerging viruses might exploit these enzymes to promote their spread. Here, we will review the proteolytic systems hijacked by SARS-CoV for S protein activation, we will discuss their contribution to viral spread in the host and we will outline antiviral strategies targeting these enzymes. This paper forms part of a series of invited articles in Antiviral Research on “From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.”
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Cites
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
Li, W., Moore, M. J., Vasilieva, N., Sui, J., Wong, S. K., Berne, M. A., Somasundaran, M., Sullivan, J. L., Luzuriaga, K., Greenough, T. C., et al. (2003) · Nature · doi:10.1038/nature02145 · Cited by 5,923
A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury
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Angiotensin-converting enzyme 2 protects from severe acute lung failure
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Matsuyama, S., Nagata, N., Shirato, K., Kawase, M., Takeda, M., & Taguchi, F. (2010) · Journal of Virology · doi:10.1128/jvi.01542-10 · Cited by 778
Cited by
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Structure, Function, and Evolution of Coronavirus Spike Proteins
Li, F. (2016) · Annual Review of Virology · doi:10.1146/annurev-virology-110615-042301 · Cited by 2,740
A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2
Chi, X., Yan, R., Zhang, J., Zhang, G., Zhang, Y., Hao, M., Zhang, Z., Fan, P., Dong, Y., Yang, Y., et al. (2020) · Science · doi:10.1126/science.abc6952 · Cited by 1,385
Molecular Architecture of the SARS-CoV-2 Virus
Yao, H., Song, Y., Chen, Y., Wu, N., Xu, J., Sun, C., Zhang, J., Weng, T., Zhang, Z., Wu, Z., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.018 · Cited by 1,060
“The activation of S requires cleavage of S1/S2 by furin-like protease and undergoes the conformational change from prefusion to postfusion (Belouzard et al., 2009; Kirchdoerfer et al., 2018; Simmons et al., 2004; Simmons et al., 2013; Song et al., 2018).”
BackgroundMolecular interaction and inhibition of SARS-CoV-2 binding to the ACE2 receptor
Yang, J., Petitjean, S. J. L., Koehler, M., Zhang, Q., Dumitru, A. C., Chen, W., Derclaye, S., Vincent, S. P., Soumillion, P., & Alsteens, D. (2020) · Nature Communications · doi:10.1038/s41467-020-18319-6 · Cited by 615
Bourdrel, T., Annesi-Maesano, I., Alahmad, B., Maesano, C. N., & Bind, M.-A. (2021) · European Respiratory Review · doi:10.1183/16000617.0242-2020 · Cited by 224
SARS-CoV-2 Infects Human Engineered Heart Tissues and Models COVID-19 Myocarditis
Bailey, A. L., Dmytrenko, O., Greenberg, L., Bredemeyer, A. L., Ma, P., Liu, J., Penna, V., Winkler, E. S., Sviben, S., Brooks, E., et al. (2021) · JACC: Basic to Translational Science · doi:10.1016/j.jacbts.2021.01.002 · Cited by 193
Furin cleavage sites naturally occur in coronaviruses
Wu, Y., & Zhao, S. (2021) · Stem Cell Research · doi:10.1016/j.scr.2020.102115 · Cited by 117
Molecular mechanisms and epidemiology of COVID-19 from an allergist’s perspective
Hosoki, K., Chakraborty, A., & Sur, S. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.05.033 · Cited by 63
Karki, N., Verma, N., Trozzi, F., Tao, P., Kraka, E., & Zoltowski, B. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041573 · Cited by 43
Metadata
- Authors
- Simmons, G., Zmora, P., Gierer, S., Heurich, A., & Pöhlmann, S.
- Venue
- Antiviral Research
- Publisher
- Elsevier BV
- Published
- 2013-12
- Volume
- 100
- Issue
- 3
- Pages
- 605-614
- ISSN
- 0166-3542 (ISSN-L)
- OpenAlex
- W2044139515
- Cited by
- 413
- References
- 4
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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