The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease
Open accessAbstract
The highly pathogenic severe acute respiratory syndrome coronavirus (SARS-CoV) poses a constant threat to human health. The viral spike protein (SARS-S) mediates host cell entry and is a potential target for antiviral intervention. Activation of SARS-S by host cell proteases is essential for SARS-CoV infectivity but remains incompletely understood. Here, we analyzed the role of the type II transmembrane serine proteases (TTSPs) human airway trypsin-like protease (HAT) and transmembrane protease, serine 2 (TMPRSS2), in SARS-S activation. We found that HAT activates SARS-S in the context of surrogate systems and authentic SARS-CoV infection and is coexpressed with the viral receptor angiotensin-converting enzyme 2 (ACE2) in bronchial epithelial cells and pneumocytes. HAT cleaved SARS-S at R667, as determined by mutagenesis and mass spectrometry, and activated SARS-S for cell-cell fusion in cis and trans , while the related pulmonary protease TMPRSS2 cleaved SARS-S at multiple sites and activated SARS-S only in trans . However, TMPRSS2 but not HAT expression rendered SARS-S-driven virus-cell fusion independent of cathepsin activity, indicating that HAT and TMPRSS2 activate SARS-S differentially. Collectively, our results show that HAT cleaves and activates SARS-S and might support viral spread in patients.
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Cites
Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
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A crucial role of angiotensin converting enzyme 2 (ACE2) in SARS coronavirus–induced lung injury
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Bats Are Natural Reservoirs of SARS-Like Coronaviruses
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Self-citationSevere acute respiratory syndrome coronavirus-like virus in Chinese horseshoe bats
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The Severe Acute Respiratory Syndrome
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Severe acute respiratory syndrome
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Cited by
Letko, M., Marzi, A., & Munster, V. (2020) · Nature Microbiology · doi:10.1038/s41564-020-0688-y · Cited by 3,109
Ou, X., Liu, Y., Lei, X., Li, P., Mi, D., Ren, L., Guo, L., Guo, R., Chen, T., Hu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15562-9 · Cited by 3,097
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
Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein
Belouzard, S., Millet, J. K., Licitra, B. N., & Whittaker, G. R. (2012) · Viruses · doi:10.3390/v4061011 · Cited by 1,368
Brann, D. H., Tsukahara, T., Weinreb, C., Lipovsek, M., Van den Berge, K., Gong, B., Chance, R., Macaulay, I. C., Chou, H.-J., Fletcher, R. B., et al. (2020) · Science Advances · doi:10.1126/sciadv.abc5801 · Cited by 1,198
Metadata
- Authors
- Bertram, S., Glowacka, I., Müller, M. A., Lavender, H., Gnirss, K., Nehlmeier, I., Niemeyer, D., He, Y., Simmons, G., Drosten, C., Soilleux, E. J., Jahn, O., Steffen, I., & Pöhlmann, S.
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2011-12-15
- Volume
- 85
- Issue
- 24
- Pages
- 13363-13372
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- OpenAlex
- W2005951184
- Cited by
- 329
- References
- 43
- FWCI
- 7.21
- Type
- journal article
- Language
- en
- Open access
- green
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- Bertram, S., Glowacka, I., Müller, M. A., Lavender, H., Gnirss, K., Nehlmeier, I., Niemeyer, D., He, Y., Simmons, G., Drosten, C., Soilleux, E. J., Jahn, O., Steffen, I., & Pöhlmann, S. (2011). Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease. Journal of Virology. https://doi.org/10.1128/jvi.05300-11
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
