CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy

Despite success in treating some hematological malignancies, CAR-T cells have not yet produced similar outcomes in solid tumors due, in part, to the tumor microenvironment, poor persistence, and a paucity of suitable target antigens. Importantly, the impact of the CAR components on these challenges...

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Main Authors: Trevor R. Baybutt, Ariana A. Entezari, Adi Caspi, Ross E. Staudt, Robert D. Carlson, Scott A. Waldman, Adam E. Snook
Format: Article
Language:English
Published: Taylor & Francis Group 2024-12-01
Series:Cancer Biology & Therapy
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Online Access:https://www.tandfonline.com/doi/10.1080/15384047.2024.2398801
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author Trevor R. Baybutt
Ariana A. Entezari
Adi Caspi
Ross E. Staudt
Robert D. Carlson
Scott A. Waldman
Adam E. Snook
author_facet Trevor R. Baybutt
Ariana A. Entezari
Adi Caspi
Ross E. Staudt
Robert D. Carlson
Scott A. Waldman
Adam E. Snook
author_sort Trevor R. Baybutt
collection DOAJ
description Despite success in treating some hematological malignancies, CAR-T cells have not yet produced similar outcomes in solid tumors due, in part, to the tumor microenvironment, poor persistence, and a paucity of suitable target antigens. Importantly, the impact of the CAR components on these challenges remains focused on the intracellular signaling and antigen-binding domains. In contrast, the flexible hinge and transmembrane domains have been commoditized and are the least studied components of the CAR. Here, we compared the hinge and transmembrane domains derived from either the CD8ɑ or CD28 molecule in identical GUCY2C-targeted third-generation designs for colorectal cancer. While these structural domains do not contribute to differences in antigen-independent contexts, such as CAR expression and differentiation and exhaustion phenotypes, the CD8ɑ structural domain CAR has a greater affinity for GUCY2C. This results in increased production of inflammatory cytokines and granzyme B, improved cytolytic effector function with low antigen-expressing tumor cells, and robust anti-tumor efficacy in vivo compared with the CD28 structural domain CAR. This suggests that CD8α structural domains should be considered in the design of all CARs for the generation of high-affinity CARs and optimally effective CAR-T cells in solid tumor immunotherapy.
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spelling doaj-art-c3e69bce597b487bb55e73a30b89f87f2025-08-20T01:58:48ZengTaylor & Francis GroupCancer Biology & Therapy1538-40471555-85762024-12-0125110.1080/15384047.2024.2398801CD8α Structural Domains Enhance GUCY2C CAR-T Cell EfficacyTrevor R. Baybutt0Ariana A. Entezari1Adi Caspi2Ross E. Staudt3Robert D. Carlson4Scott A. Waldman5Adam E. Snook6Department of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADepartment of Pharmacology, Physiology, and Cancer Biology, Sidney Kimmel Medical College, Thomas Jefferson University, Philadelphia, PA, USADespite success in treating some hematological malignancies, CAR-T cells have not yet produced similar outcomes in solid tumors due, in part, to the tumor microenvironment, poor persistence, and a paucity of suitable target antigens. Importantly, the impact of the CAR components on these challenges remains focused on the intracellular signaling and antigen-binding domains. In contrast, the flexible hinge and transmembrane domains have been commoditized and are the least studied components of the CAR. Here, we compared the hinge and transmembrane domains derived from either the CD8ɑ or CD28 molecule in identical GUCY2C-targeted third-generation designs for colorectal cancer. While these structural domains do not contribute to differences in antigen-independent contexts, such as CAR expression and differentiation and exhaustion phenotypes, the CD8ɑ structural domain CAR has a greater affinity for GUCY2C. This results in increased production of inflammatory cytokines and granzyme B, improved cytolytic effector function with low antigen-expressing tumor cells, and robust anti-tumor efficacy in vivo compared with the CD28 structural domain CAR. This suggests that CD8α structural domains should be considered in the design of all CARs for the generation of high-affinity CARs and optimally effective CAR-T cells in solid tumor immunotherapy.https://www.tandfonline.com/doi/10.1080/15384047.2024.2398801Chimeric antigen receptorCAR-T cell therapyGUCY2Ccolorectal cancer
spellingShingle Trevor R. Baybutt
Ariana A. Entezari
Adi Caspi
Ross E. Staudt
Robert D. Carlson
Scott A. Waldman
Adam E. Snook
CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
Cancer Biology & Therapy
Chimeric antigen receptor
CAR-T cell therapy
GUCY2C
colorectal cancer
title CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
title_full CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
title_fullStr CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
title_full_unstemmed CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
title_short CD8α Structural Domains Enhance GUCY2C CAR-T Cell Efficacy
title_sort cd8α structural domains enhance gucy2c car t cell efficacy
topic Chimeric antigen receptor
CAR-T cell therapy
GUCY2C
colorectal cancer
url https://www.tandfonline.com/doi/10.1080/15384047.2024.2398801
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