SARS-CoV-2 spike protein fusion transformation
From Proteopedia
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The [[SARS-CoV-2 protein S|spike protein of SARS-CoV-2]] plays a central role in [[SARS-CoV-2 spike protein priming by furin|coronavirus attachment to the ACE2 receptor on host cells]], and in getting the RNA genome of the virus into the host cell via fusion of the virus and host cell membranes, initiating infection. | The [[SARS-CoV-2 protein S|spike protein of SARS-CoV-2]] plays a central role in [[SARS-CoV-2 spike protein priming by furin|coronavirus attachment to the ACE2 receptor on host cells]], and in getting the RNA genome of the virus into the host cell via fusion of the virus and host cell membranes, initiating infection. | ||
Revision as of 00:24, 5 August 2020
This page is under construction starting August 3, 2020. This red text will be removed when the page is completed.
The spike protein of SARS-CoV-2 plays a central role in coronavirus attachment to the ACE2 receptor on host cells, and in getting the RNA genome of the virus into the host cell via fusion of the virus and host cell membranes, initiating infection.
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References
- ↑ 1.0 1.1 1.2 Cai Y, Zhang J, Xiao T, Peng H, Sterling SM, Walsh RM Jr, Rawson S, Rits-Volloch S, Chen B. Distinct conformational states of SARS-CoV-2 spike protein. Science. 2020 Jul 21. pii: science.abd4251. doi: 10.1126/science.abd4251. PMID:32694201 doi:http://dx.doi.org/10.1126/science.abd4251
- ↑ Fan X, Cao D, Kong L, Zhang X. Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein. Nat Commun. 2020 Jul 17;11(1):3618. doi: 10.1038/s41467-020-17371-6. PMID:32681106 doi:http://dx.doi.org/10.1038/s41467-020-17371-6
- ↑ Walls AC, Tortorici MA, Snijder J, Xiong X, Bosch BJ, Rey FA, Veesler D. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):11157-11162. doi:, 10.1073/pnas.1708727114. Epub 2017 Oct 3. PMID:29073020 doi:http://dx.doi.org/10.1073/pnas.1708727114
- ↑ Pabis A, Rawle RJ, Kasson PM. Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms. Proc Natl Acad Sci U S A. 2020 Mar 31;117(13):7200-7207. doi:, 10.1073/pnas.1914188117. Epub 2020 Mar 18. PMID:32188780 doi:http://dx.doi.org/10.1073/pnas.1914188117
