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bioRxiv · 10.1101/2023.11.19.567737

Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain

Abstract

CXCR4 is a ubiquitously expressed chemokine receptor that regulates leukocyte trafficking and arrest in both homeostatic and pathological states. It also participates in organogenesis, HIV-1 infection and tumor development. Despite the potential therapeutic benefit of CXCR4 antagonists, only one, plerixafor (AMD3100), which blocks the ligand-binding site, has reached the clinic. Recent advances in imaging and biophysical techniques have provided a richer understanding of the membrane organization and dynamics of this receptor. Activation of CXCR4 by CXCL12 reduces the number of CXCR4 monomers/dimers at the cell membrane and increases the formation of large nanoclusters, which are largely immobile and are required for correct cell orientation to chemoattractant gradients. Mechanistically, CXCR4 activation involves a structural motif defined by residues in TMV and TMVI. Using this structural motif as a template, we performed in silico molecular modeling followed by in vitro screening of a small compound library to identify negative allosteric modulators of CXCR4 that do not affect CXCL12 binding. We identified AGR1.137, a small molecule that abolishes CXCL12-mediated receptor nanoclustering and dynamics and blocks the ability of cells to sense CXCL12 gradients both in vitro and in vivo while preserving ligand binding and receptor internalization. Significance StatementThe chemokine receptor CXCR4 and its ligand CXCL12 are key for development, hematopoiesis, neutrophil homeostasis and lymphocyte trafficking. The only commercially available CXCR4 antagonist currently approved for clinical use is plerixafor (AMD3100), a small compound that blocks the ligand-binding site. Unfortunately, its clinical use is limited by poor pharmacokinetics and adverse effects associated with long-term administration. Here, we performed in silico analyses of a small aromatic compound library and in vitro screening to identify allosteric CXCR4 modulators. These compounds abolish the ability of cells to sense chemoattractant gradients without affecting other ligand-mediated functions such as cAMP production or receptor internalization. The selected compounds were also effective in vivo, as demonstrated by reduced tumorigenesis and metastasis in a zebrafish tumor model. Our study describes a new approach to selectively alter some GPCR functions while maintaining other functions.

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BibTeXRIS

Garcia-Cuesta, E. M., Martinez, P., Selvaraju, K., Gomez Pozo, A. M., D'Agostino, G., Gardeta, S., Quijada-Freire, A., Blanco Gabella, P., Roca, C., Jimenez-Saiz, R., Garcia-Rubia, A., Soler Palacios, B., Lucas, P., Ayala-Bueno, R., Santander Acerete, N., carrasco, y., Martinez, A., Campillo, N. E., Jensen, L. D., Rodriguez Frade, J. M., Santiago, C., Mellado, M.. 2023-11-21. Allosteric modulation of the CXCR4:CXCL12 axis by targeting receptor nanoclustering via the TMV-TMVI domain. https://doi.org/10.1101/2023.11.19.567737

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