Ibrutinib is an irreversible molecular inhibitor of ITK driving a Th1-selective pressure in T lymphocytes
Open accessAbstract
Given its critical role in T-cell signaling, interleukin-2-inducible kinase (ITK) is an appealing therapeutic target that can contribute to the pathogenesis of certain infectious, autoimmune, and neoplastic diseases. Ablation of ITK subverts Th2 immunity, thereby potentiating Th1-based immune responses. While small-molecule ITK inhibitors have been identified, none have demonstrated clinical utility. Ibrutinib is a confirmed irreversible inhibitor of Bruton tyrosine kinase (BTK) with outstanding clinical activity and tolerability in B-cell malignancies. Significant homology between BTK and ITK alongside in silico docking studies support ibrutinib as an immunomodulatory inhibitor of both ITK and BTK. Our comprehensive molecular and phenotypic analysis confirms ITK as an irreversible T-cell target of ibrutinib. Using ibrutinib clinical trial samples along with well-characterized neoplastic (chronic lymphocytic leukemia), parasitic infection (Leishmania major), and infectious disease (Listeria monocytogenes) models, we establish ibrutinib as a clinically relevant and physiologically potent ITK inhibitor with broad therapeutic utility. This trial was registered at www.clinicaltrials.gov as #NCT01105247 and #NCT01217749.
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Ibrutinib inhibits other similar kinases that contain C481, including ITK and BLK.
“Although ibrutinib inhibits other similar kinases that contain C481, including ITK and BLK,7,22”
From Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib (2014) · cites this paper as [22]
The Results confirm that ibrutinib binds and inhibits ITK, but identify its covalent binding residue as C442, not C481. The passages searched for BLK do not report BLK inhibition, so the source does not support that part of the claim. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAt relapse, none of the six patients had mutations in other kinases containing a cysteine residue homologous to C481 in BTK that are irreversibly inhibited by ibrutinib.
“At relapse, none of the patients had mutations in other kinases containing a cysteine residue homologous to C481 in BTK that are irreversibly inhibited by ibrutinib”
From Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib (2014) · cites this paper as [22]
The Introduction and Results describe cysteine-dependent irreversible inhibition of BTK and ITK, but do not report mutation testing at relapse. A search for relapsed patients, six patients, and mutations in other kinases found no passage addressing the claim. (LLM, conf=0.75)
Experimental — accuracy not yet measuredMutations have not been observed in other kinases containing C481, including ITK and BLK, in patients with acquired resistance.
“mutations have not been observed in these other targets, findings that suggest that BTK is its critical target.”
From Resistance Mechanisms for the Bruton's Tyrosine Kinase Inhibitor Ibrutinib (2014) · cites this paper as [22]
The Results describe ITK-C442A engineered in Jurkat cells to test ibrutinib binding, not mutations observed in patients with acquired resistance. Searches for acquired-resistance mutations in ITK, BLK, and other targets found no passage addressing whether such mutations were observed; our copy therefore cannot verify the attributed claim. (LLM, conf=0.73)
Experimental — accuracy not yet measured
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Self-citation
- Authors
- Dubovsky, J. A., Beckwith, K. A., Natarajan, G., Woyach, J. A., Jaglowski, S., Zhong, Y., Hessler, J. D., Liu, T.-M., Chang, B. Y., Larkin, K. M., Stefanovski, M. R., Chappell, D. L., Frissora, F. W., Smith, L. L., Smucker, K. A., Flynn, J. M., Jones, J. A., Andritsos, L. A., Maddocks, K., Lehman, A. M., Furman, R., Sharman, J., Mishra, A., Caligiuri, M. A., Satoskar, A. R., Buggy, J. J., Muthusamy, N., Johnson, A. J., & Byrd, J. C.
- Affiliations
- Department of Internal Medicine, Division of Hematology,
- The Ohio State University (US)
- Pharmacyclics (United States) (US)
- Weill Cornell Medicine (US)
- Willamette Valley Cancer Institute and Research Center (US)
- Department of Pathology, and
- ORCID
- Beckwith, Kyle A.
- Natarajan, Gayathri
- Woyach, Jennifer A.
- Jaglowski, Samantha
- Chang, Betty Y.
- Chappell, Danielle L.
- Smith, Lisa L.
- Flynn, Joseph M.
- Jones, Jeffrey A.
- Andritsos, Leslie A.
- Maddocks, Kami
- Furman, Richard
- Sharman, Jeff
- Mishra, Anjali
- Caligiuri, Michael A.
- Satoskar, Abhay R.
- Muthusamy, Natarajan
- Johnson, Amy J.
- Byrd, John C.
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2013-10-10
- Volume
- 122
- Issue
- 15
- Pages
- 2539-2549
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- PMC
- PMC3795457
- OpenAlex
- W2089103836
- Cited by
- 810
- References
- 49
- Citations by year
- 2026: 30 · 2025: 43 · 2024: 55 · 2023: 51 · 2022: 70 · 2021: 98 · 2020: 68 · 2019: 71 · 2018: 71 · 2017: 70 · 2016: 65 · 2015: 67 · 2014: 43 · 2013: 5 · 2012: 1
- FWCI
- 29.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (4p01ca081534-16)
- National Cancer Institute (P01CA095426, P50CA140158, T32CA009338, 5 T32 CA009338-33-03, P30CA016058, K12CA133250, P01-CA-081534)
- Topics
- Health Sciences › Medicine › Genetics › Chronic Lymphocytic Leukemia Research
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- ibrutinib, irreversible kinase inhibitors, Bruton's tyrosine kinase, T cell signaling, Th1 response, Th2 immune response, chronic lymphocytic leukemia, Leishmania major, Listeria monocytogenes, immunomodulation
- MeSH terms
- Adenine, Animals, Disease Models, Animal, Enzyme Inhibitors, Humans, Leukemia, Listeriosis, Lymphocyte Activation, Piperidines, Protein-Tyrosine Kinases, Pyrazoles, Pyrimidines, Leishmaniasis, Cutaneous, CD8-Positive T-Lymphocytes, Th1 Cells, Th2 Cells, Jurkat Cells, Mice, Primary Cell Culture
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