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

Nihel Ammous-Boukhris (1) , Amor Mosbah (2) , Wajdi Ayadi (1) , Emna Sahli (1) , Soizic Chevance (3) , Arnaud Bondon (3, 4) , Ali Gargouri (1) , Michele Baudy-Floc'H (3) , Raja Mokdad-Gargouri (1)

1 Université de Sfax - University of Sfax
2 ISBST - Institut Supérieur de Biotechnologie de Sidi Thabet
3 ISCR - Institut des Sciences Chimiques de Rennes
4 PRISM - Plate-forme Rennaise d'Imagerie et Spectroscopie Structurale et Métabolique

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.

Domaines: Biochimie, Biologie Moléculaire; Cancer

Nihel Ammous-Boukhris, Amor Mosbah, Wajdi Ayadi, Emna Sahli, Soizic Chevance, et al.. B1.12 a novel peptide interacting with the extracellular loop of the EBV oncoprotein LMP1. Scientific Reports, 2019, 9 (1), pp.4389. ⟨10.1038/s41598-019-39732-y⟩. ⟨hal-02086457⟩