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. | ||
| - | <StructureSection load='' size='[300,400]' side='right' caption='' scene='85/857791/Morf_6xr8_6xra_theis_lin_cao/ | + | <StructureSection load='' size='[300,400]' side='right' caption='' scene='85/857791/Morf_6xr8_6xra_theis_lin_cao/4'> |
| - | SARS-CoV-2 spike protein undergoes a dramatic conformational rearrangement (<scene name='85/857791/Morf_6xr8_6xra_theis_lin_cao/ | + | SARS-CoV-2 spike protein undergoes a dramatic conformational rearrangement (<scene name='85/857791/Morf_6xr8_6xra_theis_lin_cao/4'>restore initial scene</scene>) that plays a central role in fusing the coronavirus membrane with the host cell membrane<ref name="cai-zhang">PMID: 32694201</ref>. Similar conformational transformations have been observed for the spike protein of SARS-CoV<ref name="fan">PMID: 32681106</ref> and mouse hepatitis virus<ref name="walls">PMID: 29073020</ref>, among others. These rearrangements also have much in common with the membrane fusion mechansism of influenza hemagglutinin<ref name="pabis">PMID: 32188780</ref>. The molecular scenes in this article are based on the [[cryo-EM]] pre- and post-fusion structures of SARS-CoV-2 spike protein reported July, 2020, by Cai, Zhang and coworkers with the group of Bing Chen<ref name="cai-zhang" />. |
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Revision as of 16:17, 5 August 2020
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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
