A Cell-Based Protein-Protein Interaction Method Using a Permuted Luciferase Reporter

Haifeng Eishingdrelo*, 1, Jidong Cai 2, Paul Weissensee 2, Praveen Sharma 2, Michael J Tocci 2, Paul S Wright 3
1 BioInvenu Corporation, USA, East Hanover, NJ
2 Sanofi R&D, Bridgewater, NJ
3 Sanofi R&D, Oro Valley, AZ, USA

Article Metrics

CrossRef Citations:
Total Statistics:

Full-Text HTML Views: 443
Abstract HTML Views: 525
PDF Downloads: 201
Total Views/Downloads: 1169
Unique Statistics:

Full-Text HTML Views: 291
Abstract HTML Views: 273
PDF Downloads: 126
Total Views/Downloads: 690

© Eishingdrelo et al.; Licensee Bentham Open.

open-access license: This is an open access article licensed under the terms of the Creative Commons Attribution Non-Commercial License ( which permits unrestricted, non-commercial use, distribution and reproduction in any medium, provided the work is properly cited.

* Address correspondence to this author at the BioInvenu Corporation, USA, East Hanover, NJ, USA; Tel: 973-585-6777; Fax: 973-585-6776; E-mail:


We have developed a novel cell-based protein-protein interaction assay method. The method relies on conversion of an inactive permuted luciferase containing a Tobacco Etch Virus protease (TEV) cleavage sequence fused onto protein (A) to an active luciferase upon interaction and cleavage by another protein (B) fused with the TEV protease. We demonstrate assay applicability for ligand-induced protein-protein interactions including G-protein coupled receptors, receptor tyrosine kinases and nuclear hormone receptors.

Keywords: Cell-based assay, permuted luciferase, protein-protein interactions, GPCR, NHR, RTK, cell signaling, beta-arrestins.