Proteopedia

Coronavirus Disease 2019 (COVID-19)


SARS-CoV-2 virus. The spikes, that adorn the virus surface, impart a corona like appearance (Fusion Animation).

A novel coronavirus SARS-CoV-2, detected in Wuhan, China in 2019, was found to cause severe respiratory illness named COVID-19[1] (COrona VIrus Disease-2019).

There’s a new NCBI site on COVID-19/SARS-CoV-2. It will help bench scientists, bioinformaticians, clinicians & others connect with information they need to study SARS-CoV-2 and end the pandemic.

A video (by Elara) shows how the virus interacts with its human (host) cells, via its spike proteins[2][3][4][5][6][7], thus permitting the viral genome to enter its host & begin infection. The spike protein is induced for optimal binding when it is clipped by a protease (see animation on right side) and more details at SARS-CoV-2_protein_S_activation_by_furin. Subsequently, it undergoes a dramatic transformation to induce membrane fusion and infection, explained with a morph animation at SARS-CoV-2 spike protein fusion transformation.


Useful sites on COVID-19

  • A plot of the Biweekly change in confirmed COVID-19 cases throughout the world

Clicking the above image goes to the Our World in Data site with the most recent data.

  • COVID-19 AlphaFold2 Models that have been of structures of SARS CoV-2 proteins whose structure have not yet been experimentally determined.


References

  1. ↑ Naming the coronavirus disease (COVID-19) and the virus that causes it
  2. ↑ Pillay TS. Gene of the month: the 2019-nCoV/SARS-CoV-2 novel coronavirus spike protein. J Clin Pathol. 2020 Jul;73(7):366-369. doi: 10.1136/jclinpath-2020-206658. Epub, 2020 May 6. PMID:32376714 doi:http://dx.doi.org/10.1136/jclinpath-2020-206658
  3. ↑ Wrapp D, Wang N, Corbett KS, Goldsmith JA, Hsieh CL, Abiona O, Graham BS, McLellan JS. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020 Feb 19. pii: science.abb2507. doi: 10.1126/science.abb2507. PMID:32075877 doi:http://dx.doi.org/10.1126/science.abb2507
  4. ↑ Walls AC, Park YJ, Tortorici MA, Wall A, McGuire AT, Veesler D. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 2020 Mar 6. pii: S0092-8674(20)30262-2. doi: 10.1016/j.cell.2020.02.058. PMID:32155444 doi:http://dx.doi.org/10.1016/j.cell.2020.02.058
  5. ↑ Wrobel AG, Benton DJ, Xu P, Roustan C, Martin SR, Rosenthal PB, Skehel JJ, Gamblin SJ. SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects. Nat Struct Mol Biol. 2020 Jul 9. pii: 10.1038/s41594-020-0468-7. doi:, 10.1038/s41594-020-0468-7. PMID:32647346 doi:http://dx.doi.org/10.1038/s41594-020-0468-7
  6. ↑ Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol. 2002 Oct;3(10):753-66. doi: 10.1038/nrm934. PMID:12360192 doi:http://dx.doi.org/10.1038/nrm934
  7. ↑ Wang Q, Zhang Y, Wu L, Niu S, Song C, Zhang Z, Lu G, Qiao C, Hu Y, Yuen KY, Wang Q, Zhou H, Yan J, Qi J. Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2. Cell. 2020 Apr 7. pii: S0092-8674(20)30338-X. doi: 10.1016/j.cell.2020.03.045. PMID:32275855 doi:http://dx.doi.org/10.1016/j.cell.2020.03.045

Morph showing the transition of SARS-CoV-2 spike protein from its closed to open conformation induced by proteolytic cleavage, details at SARS-CoV-2_spike_protein_priming_by_furin

Drag the structure with the mouse to rotate

ReferencesReferences

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