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ALONSO, R.

Publications and source records attributed to ALONSO, R..

2 recordsLinked to original sources

CAR-MACROPHAGES ACTIVATE ANTI TUMOR T CELLS IN THE ABSENCE OF PHAGOCYTOSIS

Macrophages are highly abundant within the tumor microenvironment and serve as an essential bridge between innate and adaptive immune responses. Thus, they have emerged as promising candidates for chimeric antigen receptor (CAR)-based therapeutic strategies. Previous studies demonstrated that adenovirally-transduced CAR-macrophages (CAR-M), used in clinical trials, can perform tumor cell phagocytosis, reshape the tumor microenvironment towards a proinflammatory state, and promote host T cell activation. However, how early interactions between CAR-M and tumor cells shape subsequent T cell effector functions remains poorly understood. Particularly, uncoupling the adenoviral-induced proinflammatory phenotype from CAR-M effector functions remains to be dissected. Here, using phagocytosis-optimized CAR-Ms, we demonstrated that T cells are crucial mediators of CAR-M therapeutic efficacy. Mechanistically, we identify that CAR-M-derived cytokines and chemokines are key drivers of T cell functions while antigen cross presentation appears largely dispensable. Dynamic imaging of CAR-M-tumor cell interactions revealed heterogenous phagocytic abilities, regardless of contact duration. Finally, we show that non-phagocytic interactions can instruct pro-inflammatory macrophage repolarization and subsequent T cell activation. Altogether, these findings define an alternative mode of CAR-M action in which CAR engagement alone, independently of target cell uptake, is sufficient to enhance T cell functions. Our study underscores the importance of non-phagocytic CAR signaling as an additional mechanism for CAR-M effector functions opening new avenues for the design of next generation CAR for macrophage-based therapies.

immunology↗

Membrane-penetrating peptide from the translocation region of Bordetella Adenylate Cyclase Toxin prevents toxin cytotoxicity on target cells

Adenylate cyclase toxin (ACT) is one of the main virulence factors of Bordetella pertussis, with crucial role in colonization of human respiratory tract. ACT toxicity on target phagocytes results from translocation of its adenylate cyclase domain and production of high cAMP levels and from pore formation. Recently, we unveiled in ACT four cholesterol-recognition motifs involved in specific interaction with membrane cholesterol, which might stabilize membrane topology of critical helices for ACT activity. Here we explore an amphipathic peptide corresponding to ACT residues 454 to 487 containing one of such CRAC motifs. We show that P454-487 penetrates into DOPC vesicles as a long and tilted -helix, while in cholesterol presence experiments conformational changes that critically depend on the CRAC Phe-485 residue. Moreover, P454-487 is capable of blocking ACT toxicity on cells by outcompeting with the full-length toxin for membrane binding. We anticipate P454-487 may have potential clinical applicability in controlling Bordetella infection.

biophysics↗