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| Title | Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 3433, Year 2021 |
| Publish date | Jun 8, 2021 |
 Authors | Jin Chai / Yuanheng Cai / Changxu Pang / Liguo Wang / Sean McSweeney / John Shanklin / Qun Liu /  |
| PubMed Abstract | The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which ...The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which occurs through viral protein recognition of human targets. To understand the structural basis for SARS-CoV-2 viral-host protein recognition, here we use cryo-electron microscopy (cryo-EM) to determine a complex structure of the human cell junction protein PALS1 and SARS-CoV-2 viral envelope (E) protein. Our reported structure shows that the E protein C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains of PALS1. Our structural analysis provides an explanation for the observation that the viral E protein recruits PALS1 from lung epithelial cell junctions. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1-E interactions to reduce E-mediated virulence. |
 External links | Nat Commun / PubMed:34103506 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.65 Å |
| Structure data | EMDB-23665, PDB-7m4r: |
| Source |
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 Keywords | CELL ADHESION/VIRAL PROTEIN / SARS-CoV-2 envelope protein / PDZ-binding motif /  complex / pathogen-host interaction / CELL ADHESION-VIRAL PROTEIN complex |
