Motif-based SARS-CoV-2 protein-human protein interactions as potential antiviral target sites biorxivpreprint uppsalauni SARSCoV2 COVID19 Antiviral AntiviralTarget
By Pooja Toshniwal PahariaOct 13 2022Reviewed by Aimee Molineux In a recent study posted to the bioRxiv* preprint server, researchers performed a ProP-PD analysis to identify peptides from intrinsically disordered human proteome regions that bind with severe acute respiratory syndrome coronavirus 2 genome-encoded folded protein domains .
PD expression constructs were created from SARS-CoV-2 proteins , of which 26 PDs were used for ProP-PD phage display selection screen analysis against the human disorderome peptide library. The HD2 library displayed amino acid overlapping peptides in the host proteome’s disordered sites on the M13 phage surface.
Results Eleven folded PDs of the SARS-CoV-2 genome were bound to human genome peptides. Out of 281 high/medium peptides, 239 host proteins were found to interact with SARS-CoV-2 PDs including Nsp1,3,5,8,9, and 16, Ubl1, adipocyte differentiation-related protein , SUD-M, open reading frame -8, 9b and nucleocapsid protein N-terminal domain .
The FP analysis of 23 peptide-peptide interactions involving eight SARS-CoV-2 PDs showed binding affinities in the micromolar range. The leucine residues at P1 , with tyrosine residues at P5, were essential for binding, indicating that the Nsp3 Ubl1 binding motif in NCOA21074-1089 was LxxxY. Enrichment of ligands associated with transcriptional regulation processes was observed.
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