Sandbox Reserved 1736
From Proteopedia
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Initially, when the virus begins to interact with the host cell, this causes structural rearrangement of the S protein.<ref>Suzuki, Y. J.; Gychka, S. G. SARS-COV-2 Spike Protein Elicits Cell Signaling in Human Host Cells: Implications for Possible Consequences of Covid-19 Vaccines. Vaccines '''2021''', 9 (1), 36.</ref> The rearrangement of the S protein then allows the virus to be able to fuse with the host cell membrane. The spikes of the protein are coated with polysaccharide molecules to be able to act like a form of camouflage. This allows for the host immune system to not bind to the spikes during entry. | Initially, when the virus begins to interact with the host cell, this causes structural rearrangement of the S protein.<ref>Suzuki, Y. J.; Gychka, S. G. SARS-COV-2 Spike Protein Elicits Cell Signaling in Human Host Cells: Implications for Possible Consequences of Covid-19 Vaccines. Vaccines '''2021''', 9 (1), 36.</ref> The rearrangement of the S protein then allows the virus to be able to fuse with the host cell membrane. The spikes of the protein are coated with polysaccharide molecules to be able to act like a form of camouflage. This allows for the host immune system to not bind to the spikes during entry. | ||
| - | <scene name='91/919045/Nc_sars-cov-2_spike_protein/2'> | + | <scene name='91/919045/Nc_sars-cov-2_spike_protein/2'>N-terminus (blue) to C-terminus (red)</scene> |
== Mutations == | == Mutations == | ||
The viral DNA experiences numerous spike protein changes to enable it to infect a new mammalian host and leap species. The <scene name='91/919045/D614g_sars-cov-2_spike_protein/1'>D614G mutation</scene> is a common mutation in SARS-CoV-2 spike protein. It has no effect on the affinity of monomeric spike protein for ACE2 and residue 614 is found outside the receptor binding domain (RBD). The mutation dramatically increases the virus's capacity to infect and spread. <ref>Jackson, C. B.; Zhang, L.; Farzan, M.; Choe, H. Functional Importance of the D614G Mutation in the SARS-COV-2 Spike Protein. Biochemical and Biophysical Research Communications 2021, 538, 108–115.</ref> Drugs created to target protein-protein interactions, such as vaccines, may be affected by mutations found at the interface between the ACE2 receptor and the spike protein. | The viral DNA experiences numerous spike protein changes to enable it to infect a new mammalian host and leap species. The <scene name='91/919045/D614g_sars-cov-2_spike_protein/1'>D614G mutation</scene> is a common mutation in SARS-CoV-2 spike protein. It has no effect on the affinity of monomeric spike protein for ACE2 and residue 614 is found outside the receptor binding domain (RBD). The mutation dramatically increases the virus's capacity to infect and spread. <ref>Jackson, C. B.; Zhang, L.; Farzan, M.; Choe, H. Functional Importance of the D614G Mutation in the SARS-COV-2 Spike Protein. Biochemical and Biophysical Research Communications 2021, 538, 108–115.</ref> Drugs created to target protein-protein interactions, such as vaccines, may be affected by mutations found at the interface between the ACE2 receptor and the spike protein. | ||
Revision as of 23:53, 8 December 2022
Structure
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References
- ↑ Weisblum, Y.; Schmidt, F.; Zhang, F.; DaSilva, J.; Poston, D.; Lorenzi, J. C. C.; Muecksch, F.; Rutkowska, M.; Hoffmann, H.-H.; Michailidis, E.; Gaebler, C.; Agudelo, M.; Cho, A.; Wang, Z.; Gazumyan, A.; Cipolla, M.; Luchsinger, L.; Hillyer, C. D.; Caskey, M.; Robbiani, D. F.; Rice, C. M.; Nussenzweig, M. C.; Hatziioannou, T.; Bieniasz, P. D. Escape from Neutralizing Antibodies by SARS-COV-2 Spike Protein Variants. eLife 2020, 9.
- ↑ 2.0 2.1 Bangaru, S.; Ozorowski, G.; Turner, H. L.; Antanasijevic, A.; Huang, D.; Wang, X.; Torres, J. L.; Diedrich, J. K.; Tian, J.-H.; Portnoff, A. D.; Patel, N.; Massare, M. J.; Yates, J. R.; Nemazee, D.; Paulson, J. C.; Glenn, G.; Smith, G.; Ward, A. B. Structural Analysis of Full-Length SARS-COV-2 Spike Protein from an Advanced Vaccine Candidate. Science 2020, 370 (6520), 1089–1094.
- ↑ Xia, X. Domains and Functions of Spike Protein in SARS-COV-2 in the Context of Vaccine Design. Viruses 2021, 13(1).
- ↑ 4.0 4.1 Huang, Y.; Yang, C.; Xu, X.-feng; Xu, W.; Liu, S.-wen. Structural and Functional Properties of SARS-COV-2 Spike Protein: Potential Antivirus Drug Development for Covid-19. Acta Pharmacologica Sinica 2020, 41 (9), 1141–1149.
- ↑ Suzuki, Y. J.; Gychka, S. G. SARS-COV-2 Spike Protein Elicits Cell Signaling in Human Host Cells: Implications for Possible Consequences of Covid-19 Vaccines. Vaccines 2021, 9 (1), 36.
- ↑ Jackson, C. B.; Zhang, L.; Farzan, M.; Choe, H. Functional Importance of the D614G Mutation in the SARS-COV-2 Spike Protein. Biochemical and Biophysical Research Communications 2021, 538, 108–115.
- ↑ Guruprasad, L. Human Sars-CoV‐2 Spike Protein Mutations. Proteins: Structure, Function, and Bioinformatics 2021, 89 (5), 569–576.
- ↑ Berger, I.; Schaffitzel, C. The Sars-COV-2 Spike Protein: Balancing Stability and Infectivity. Cell Research 2020, 30 (12), 1059–1060.
- ↑ Zhou, T.; Tsybovsky, Y.; Gorman, J.; Rapp, M.; Cerutti, G.; Chuang, G.-Y.; Katsamba, P. S.; Sampson, J. M.; Schön, A.; Bimela, J.; Boyington, J. C.; Nazzari, A.; Olia, A. S.; Shi, W.; Sastry, M.; Stephens, T.; Stuckey, J.; Teng, I.-T.; Wang, P.; Wang, S.; Zhang, B.; Friesner, R. A.; Ho, D. D.; Mascola, J. R.; Shapiro, L.; Kwong, P. D. Cryo-EM Structures of SARS-COV-2 Spike without and with Ace2 Reveal a Ph-Dependent Switch to Mediate Endosomal Positioning of Receptor-Binding Domains. Cell Host & Microbe 2020, 28 (6).
