Phage-display screening identifies LMP1-binding peptides targeting the C-terminus region of the EBV oncoprotein

Ammous-Boukhris, Nihel; Mosbah, Ahmed; Sahli, Emna; Ayadi, Wajdi; Hadhri-Guiga, Boutheina; Chérif, Ameur; Gargouri, Ali; Mokdad-Gargouri, Raja

doi:10.1016/j.peptides.2016.09.008

Cited by 3 publications

(1 citation statement)

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“…A total of five three-dimensional structure models were generated by GPCR-I-TASSER, among them, the best model was identified based on confidence score (C-Score) and the refined model coordinates were evaluated by MolProbity 34 . As the LMP1 atomic level structural data was not yet available, we constructed a model as described in our previous work 35 , and the B1.12 peptide model was generated similarly (all models are available as Supplementary Materials). To obtain a better understanding of the interaction between the N-terminal domain of LMP1 and the B1.12 peptide, we performed the modeling of the peptides binding to LMP1 in order to predict the positions and the orientation of the peptides in her binding cleft.…”

Section: Methodsmentioning

confidence: 99%

B1.12: a novel peptide interacting with the extracellular loop of the EBV oncoprotein LMP1

Ammous-Boukhris

Mosbah

Ayadi

et al. 2019

Sci Rep

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Latent membrane protein 1 (LMP1) encoded by the Epstein-Barr virus (EBV) plays an important role in EBV-induced cell transformation. Down-regulation of the LMP1 expression had shown promising results on cancer cell therapy. In this study, we identified by Phage display a novel peptide called B1.12 (ACPLDLRSPCG) which selectively binds to the extracellular loop (B1) of the LMP1 oncoprotein as demonstrated by molecular docking, NMR and ITC. Using an LMP1 expressing cell line, we showed that B1.12 decreased cell viability, and induced G0/G1 cell cycle arrest. In addition, the expression of A20, pAkt, and pNFkb (pRelA536) in C666-1 cells treated with B1.12 decreased compared to the untreated cells. In conclusion, we selected a novel peptide able to bind specifically to the extracellular loop of LMP1 and thus modulate its oncogenic properties.

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Section: Methodsmentioning

confidence: 99%