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==Spike glycoprotein==
==Spike glycoprotein==
<StructureSection load='6VSB' size='340' side='right' caption='3D representation of the Spike glycoprotein' scene=''>
<StructureSection load='6VSB' size='340' side='right' caption='3D representation of the Spike glycoprotein' scene=''>
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3D structure representation of the Spike glycoprotein<ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref>.
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3D structure representation of the Spike glycoprotein<ref>DOI 10.1002/ijch.201300024</ref> <ref>PMID:21638687</ref>.
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The S-protein of SARS-CoV-2 expressed by the ORF1b gene is trimeric in structure, where each monomer is 180 kDa in size and has two main subunits, an S1 and an S2 subunit. S1 subunit attaches itself to the host cell angiotensin-converting enzyme 2 (ACE2) transmembrane protein. S2 subunit acts in the fusion process of the S-protein which is done by the cleavage protease transmembrane serine or furin <ref>Mohammad, A., Alshawaf, E., Marafie, S. K., Abu-Farha, M., Abubaker, J., & Al-Mulla, F. (2020). Higher binding affinity of Furin to SARS-CoV-2 spike (S) protein D614G could be associated with higher SARS-CoV-2 infectivity. International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases, S1201-9712(20)32237-2. Advance online publication. https://doi.org/10.1016/j.ijid.2020.10.033
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==Disease==
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==Introduction==
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The Spike protein is related to the novel coronavirus pandemic discovered in 2019. The virus is named as the severe acute respiratory syndrome coronavirus 2 (SARS-COV-2) and it belongs to the β coronavirus family. The SARS-COV-2 is a single stranded RNA with 29,881bp length, which encodes for 9860 amino acids. It is compose of two proteins: the structural and non-structural proteins. The structural proteins are S,E,M and N ; whiles as the non-structural proteins are encoded on the ORF regions.
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The spike glycoprotein is associated with the noval human COV2 responsible for severe acute respiratory syndrome (SARS).The s-protein froms the sructural protein of the SARS-COV-2 virus which gives it crown-like from.
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==The Spike Protein==
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The S-protein is a structural protein extends from the viral membrane and it is uniformly arranged as a trimer on the surface to give the crown-like appearance of the SARS-COV-2. The Spike protein is 14-1255bp long, which mediates a receptor binding and fusion of the virus and a cellular membrane. Is also gives the virus its name in Latin as "Corona".
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== Function ==
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==Domains==
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SARS-COV-2 utilizes s-protein to facilitate attachment to host cell surface membranes.
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The S-protein of the SARS-COV-2 has two main subunits , an S1 and S2 subunits. The S1 subunit is located on residue #14–685 ( contains the NTD) and interact with human AEC2 by attaching its virion to the cell membrane by interacting with host receptor. The S2 subunit is located on residue #686–1273 ( contains the CT) which serves as the fusion protein of the virus.
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==Activation of S-protein==
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Before the Spike protein can be activated , it has to be cleaved by the protease Furin protein.
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== Relevance ==
 
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The two subunits of the s-protein ; S1 and S2 interact with other proteins like the 3a and 7a on the SARS-COV-2. The s-protein has other protein modifications such as the amino acid modification in which there is a disulfide bond, Glycosylation with an N-liked to asparagine of the host cell . There is also a post-translation modification where the Spike glycoprotein is digested within host endosomes.
 

Revision as of 03:56, 16 November 2020

Spike glycoprotein

3D representation of the Spike glycoprotein

Drag the structure with the mouse to rotate

References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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