Figure 4

The SARS CoV-2 spike domain, RGD and integrin binding effect-relationship for vaccine design strategy

Luisetto M*, Tarro G, Khaled Edbey, Almukthar N, Cabianca L, Mashori GR, Yesvi AR and Latyschev OY

Published: 20 July, 2021 | Volume 5 - Issue 1 | Pages: 027-041

apb-aid1014-g004

Figure 4:

SARS-CoV-2)contains 4 major structure proteins: spike (S), membrane (M) and envelope (E) proteins, which are embedded on the virion -surface, and nucleocapsid (N) protein, which binds viral -RNA inside the virion. The S- protein trimer in its pre-fusion conformation is shown. The S- protein comprises the S1 subunit (which includes the N-terminal domain (NTD) and the receptor-binding domain (RBD)) (the receptor-binding motif (RBM) within the RBD is also labelled) and the S2 subunit (which includes fusion peptide (FP), connecting- region (CR), heptad repeat 1 (HR1), heptad repeat (HR2) and central- helix (CH)). The SARS-CoV-2 S protein binds to its host- receptor, the dimeric human angiotensin-converting enzyme 2 (hACE2), via the RBD and dissociates the S1- subunits. Cleavage at both S1–S2 and S2′ sites allows structural re-arrangement of the S2 subunit required for virus–host membrane fusion. The S2-trimer in its post-fusion arrangement is shown. The RBD is an attractive vaccine- target. The generation of an RBD-dimer or RBD-trimer has been shown to enhance the immune-genicity of RBD-based vaccines. A stabilized S-trimer shown with a C-terminal trimer-tag is a vaccine target. The pre-fusion S protein is generally metastable during in vitro preparations and prone to transform into its post-fusion conformation. Mutation of 2 residues (K986 and V987) to proline stabilizes S- protein (S-2P) and prevents the pre-fusion to post-fusion structural- change.

Read Full Article HTML DOI: 10.29328/journal.apb.1001014 Cite this Article Read Full Article PDF

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