IP Library Granted Patent US 12,221,465
Granted Patent B2
US 12,221,465 · App. 16/122,562 · Granted Feb 11, 2025

Signaling and antigen-presenting bifunctional receptors (SABR)

Inventors: Alok V Joglekar (Pasadena, CA); Michael T Leonard (Pasadena, CA); Michael T Bethune (Pasadena, CA); David Baltimore (Pasadena, CA)
Assignee: California Institute of Technology
C07K14/7051A61K39/4611A61K39/4615A61K39/4621A61K39/4622A61K39/4632A61K39/46433A61K39/464401A61K39/464488A61K39/464491A61K39/464838A61P37/00C07K14/705C07K14/70539C12N5/0636C40B40/02G01N33/566G01N33/68A61K38/00C07K2319/03C07K2319/70G01N2333/7051
View Patent ↗
Loading inventors, assignments & file history…
Monitor This Case
Get email alerts when status or documents change.
Order Certified Copies
Most orders are placed with the USPTO same day — all within 24 business hours.
Order via The Patent Place →
Pre-filled with this patent's details
Quick Facts
Patent No.
US 12,221,465
App. No.
16/122,562
Granted
Feb 11, 2025
Kind
B2
Abstract

Described herein are compositions and methods for signaling and antigen-presenting bifunctional receptors (SABRs) comprising one or more antigen presenting domains; and one or more signal transduction domains, wherein the one or more antigen presenting domains comprise a binding fragment of a major histocompatibility complex (MHC) molecule. Various immunological functions of the SABRs are also described.

Claims (26)

1. A signaling and antigen-presenting bifunctional receptor (SABR) comprising:

an antigen presenting domain comprising a binding domain of a major histocompatibility complex (MHC) molecule, a peptide epitope covalently linked to the binding domain of the MHC molecule for extracellular presentation of the peptide epitope to a first cell expressing at least one antigen receptor, and a transmembrane domain;

one or more linkers; and

a signal transduction domain fused to the antigen presenting domain, wherein the SABR is made by a method comprising expressing, in a second cell that is an isolated cell, a nucleic acid sequence encoding the antigen presenting domain, the signal transduction domain, and the one or more linkers, and

wherein the peptide epitope is synthesized and cloned, from pooled single stranded oligonucleotide libraries, into the nucleic acid sequence,

wherein the transmembrane domain comprises a transmembrane domain from one or more of 4-1BB (CD137), CD28, CD27, DAP10, ICOS, OX40, PD1, CTLA4, TIM3, CD3zeta, Notch, synNotch, CD79A, CD79B, CD72, CD22, CD5, CD19, CD45, IL2, IL4, EPO, GM-CSF, JAK-STAT, CCL10, a G protein coupled receptor, a receptor of the TNF Receptor superfamily, a NK cell receptor, a Fc receptor, a toll-like receptor, a RIG-I-like receptor, a NOD-like receptor, or a MHC molecule, and

wherein the signal transduction domain comprises an intracellular signaling domain of CD137, CD27, DAP10, ICOS, OX40, PD1, CTLA4, TIM3, an IL2, an IL4, an EPO, a GM-CSF, JAK-STAT, a CCL10, a G protein coupled receptor, or a receptor of the TNF Receptor superfamily, or a fragment thereof.

2. The SABR of claim 1 , wherein the antigen presenting domain comprises the MHC.

3. The SABR of claim 1 , wherein the MHC comprises a Class I MHC, and

wherein the MHC comprises HLA-A*0201 or HLA-B*2705.

4. The SABR of claim 1 , wherein the MHC comprises a Class II MHC.

5. The SABR of claim 1 , wherein the second cell is a reporter cell, and

wherein the reporter cell provides a detectable marker upon binding of the SABR to the antigen receptor.

6. The SABR of claim 5 , wherein the reporter cell comprises NFAT-GFP-Jurkat cells.

7. The SABR of claim 5 , wherein the first cell is a T cell comprising TCR.

8. The SABR of claim 5 , wherein the first cell expresses an orphan TCR.

9. The SABR of claim 1 , wherein the oligonucleotide libraries encode pathogen epitopes.

10. A signaling and antigen-presenting bifunctional receptor (SABR) comprising:

an antigen presenting domain comprising a major histocompatibility complex (MHC) molecule, a peptide epitope covalently linked to the MHC molecule for extracellular presentation of the peptide epitope to a first cell expressing at least one antigen receptor, and a transmembrane domain;

one or more linkers; and

a signal transduction domain fused to the antigen presenting domain,

wherein the SABR is made by a method comprising expressing, in a second cell that is an isolated cell, a nucleic acid sequence encoding the antigen presenting domain and the signal transduction domain, wherein the MHC molecule is class I or class II,

wherein the peptide epitope is synthesized and cloned, from pooled single stranded oligonucleotide libraries, into the nucleic acid sequence,

wherein the peptide epitope comprises a cancer peptide epitope,

wherein the transmembrane domain comprises a transmembrane domain from one or more of 4-1BB (CD137), CD28, CD27, DAP10, ICOS, OX40, PD1, CTLA4, TIM3, CD3zeta, Notch, synNotch, CD79A, CD79B, CD72, CD22, CD5, CD19, CD45, IL2, IL4, EPO, GM-CSF, JAK-STAT, CCL10, a G protein coupled receptor, a receptor of the TNF Receptor superfamily, a NK cell receptor, a Fc receptor, a toll-like receptor, a RIG-I-like receptor, a NOD-like receptor, or an MHC molecule, and

wherein the signal transduction domain comprises an intracellular signaling domain of CD137, CD27, DAP10, ICOS, OX40, PD1, CTLA4, TIM3, an IL2, an IL4, an EPO, a GM-CSF, JAK-STAT, a CCL10, a G protein coupled receptor, or a receptor of the TNF Receptor superfamily, or a fragment thereof.

Assignments (1)
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Oct 7, 2024
From: JOGLEKAR, ALOK V.; LEONARD, MICHAEL T.; BETHUNE, MICHAEL T.; BALTIMORE, DAVID
To: CALIFORNIA INSTITUTE OF TECHNOLOGY
Reel/Frame 068816/0085 →
Continuity (2)
Provisional Application 62554652 · Sep 6, 2017
Related Publication 20190201443A1 · Jul 4, 2019
References Cited (49)
US 6491908B1 · Rosenberg · 2002 [cited by applicant]
US 7319143B2 · Gross · 2008 [cited by third party]
US 20040137562A1 · Gross et al. · 2004 [cited by applicant]
US 20070066802A1 · Geiger · 2007 [cited by third party]
US 20150139943A1 · Campana · 2015 [cited by examiner]
WO WO0191698A2 · 2001 [cited by applicant]
WO WO0191698A3 · 2001 [cited by applicant]
WO WO2014127261 · 2014 [cited by applicant]
WO WO2016097334A1 · 2016 [cited by applicant]
WO WO2016168773 · 2016 [cited by applicant]
WO WO2017070608 · 2017 [cited by applicant]
WO WO201717332 · 2017 [cited by examiner]
HLA Nomenclature (2015) (Year: 2015). [cited by examiner]
Liu et al.(MHC Complex: Interaction with Peptides. In: eLS. John Wiley & Sons, Ltd: Chichester, DOI: 10.1002/9780470015902.a0000922.pub2, 2011, pp. 1-12) (Year: 2011). [cited by examiner]
Wieczorek et al (Front. Immunol. 2017, vol. 8, article 292: 1-16) (Year: 2017). [cited by examiner]
Ali-Khan et al.(Current Protocols in Protein Science, 2002: 22.1.-22.1.19) (Year: 2002). [cited by examiner]
Schumacher and Schrieber (Science, 2015, 384 (6230): 69-74) (Year: 2015). [cited by examiner]
Celis et al.(PNAS USA, 1994, 91: 2105-2109) (Year: 1994). [cited by examiner]
Ochoa-Garay et al.(Mol. Immunol. 1997, 34(3): 273-281) (Year: 1997). [cited by examiner]
Shen et al (J. Immunol. 2008, 180: 3601-3611). (Year: 2008). [cited by examiner]
Novellino et al (Cancer Immunol. Immunother. 2005, 54: 187-207) (Year: 2005). [cited by examiner]
Jackaman et al (Cancer Immunol. Immunother., 2012, 61: 2343-2356) (Year: 2012). [cited by examiner]
Ennis et al (Virology, 1999, 259: 256-261) (Year: 1999). [cited by examiner]
Aarnoudse et al (Int. J. Cancer, 2002, 99: 7-13) (Year: 2002). [cited by examiner]
Hutloff et al (Nature, 1999, 397: 263-266) (Year: 1999). [cited by examiner]
Rudolf et al (Clin. Cancer Res., Mar. 2001; 7(3 Suppl): 788s-795s, abstract) (Year: 2001). [cited by examiner]
Extended European Search Report and Written Opinion in corresponding European Patent Application No. 18854825.9, dated Mar. 31, 2021 in 9 pages. [cited by applicant]
Moisini et al., “Redirecting Therapeutic T Cells against Myelin-Specific T Lymphocytes Using a Humanized Myelin Basic Protein-HLA-DR2-3 Chimeric Receptor”, The Journal of Immunology, Feb. 21, 2008, vol. 180, No. 5, pp. … [cited by applicant]
Jyothi et al., “Targeting autoantigen-specific T cells and suppression of autoimmuneencephalomyelitis with receptor-modified T lymphocytes”, Nature Biotechnology, Nov. 11, 2002, vol. 20, No. 12, pp. 1215-1220. [cited by applicant]
Joglekar et al., “T ce11 antigen discovery via signaling and antigen-presenting bifunctional receptors”, Nature Methods, Jan. 28, 2019, vol. 16, No. 2, pp. 191-198. [cited by applicant]
Nguyen et al., “Identification of a murine CD28 dileucine motif that suppresses single-chain chimeric T-cell receptor expression and function”, Blood, Dec. 15, 2003, vol. 102, No. 13, pp. 4320-4325. [cited by applicant]
Geiger et al., “The TCR ζ-Chain Immunoreceptor Tyrosine-Based Activation Motifs AreSufficient for the Activation and Differentiation of Primary T Lymphocytes”, The Journal Of Immunology, Jan. 1, 1999, vol. 162, pp. 5931… [cited by applicant]
Nguyen et al., “Antigen specific targeting of CD8+ T cells with receptor-modified T lymphocytes”, Gene Therapy, Apr. 1, 2003, vol. 10, No. 7, pp. 594-604. [cited by applicant]
Geiger et al., “Integrated src kinase and costimulatory activity enhances signal transduction through single-chain chimeric receptors in T lymphocytes”, Blood, Jan. 15, 2001, vol. 98, No. 8, pp. 2364-2371. [cited by applicant]
Cole, D. K. et al., “T-cell receptor (TCR)-peptide specificity overridesaffinity-enhancing TCR-major histocompatibility complex interactions”, The Journal of Biological Chemistry, Jan. 10, 2014, vol. 289, No. 2, pp. 628… [cited by applicant]
Reiser, J.-B. et al., “Analysis of relationships between peptide/MHCstructural features and naive T cell frequency in humans”, The Journal of Immunology, 2014, vol. 193, pp. 5816-5826. [cited by applicant]
International Search Report of PCT/US2018/049622 dated Dec. 28, 2018 in 5 pages. [cited by applicant]
Written Opinion of PCT/US2018/049622 dated Dec. 28, 2018 in 7 pages. [cited by applicant]
Office Action for CN 201880071856.4, issued Nov. 2, 2022, 15 pages. [cited by applicant]
Office Action for JP 2020-513554, issued Nov. 22, 2022, 14 pages. [cited by applicant]
Office Action issued in JP 2020-513554 issued Apr. 25, 2023, 10 pages. [cited by applicant]
Office Action issued in CN 201880071856.4 issued Sep. 16, 2023, 14 pages. [cited by applicant]
Office Action issued in CN 201880071856.4 issued Dec. 21, 2023, 14 pages. [cited by applicant]
Zhang, Tong et al., “SING: a novel strategy for identifying tumor-specific, CTL-recognized tumor antigens” The FASEB Journal, Mar. 2004, pp. 600-602, vol. 18, Issue 3. [cited by applicant]
Office Action for JP 2020-513554 issued May 17, 2022, 13 pages. [cited by applicant]
Geiger et al., Integrated src kinase and costimulatory activity enhances signal transduction through single-chain chimeric receptors in T lymphocytes, Blood, 2001, 98:2364-2371. [cited by third party]
Jyothi et al., Targeting autoantigen-specific T cells and suppression of autoimmune 2 encephalomyelitis with receptor-modified T lymphocytes, Nat. Biotechnol., 2002, 20:1215-1220. [cited by third party]
Nguyen P. and Geiger T.L., Antigen-specific targeting of CD8+ T cells with receptor-modified T lymphocytes, Gene Therapy, 2003, 10:594-604. [cited by third party]
Margalit et al., Chimeric β2 microglobulin/CD3ζ polypeptides expressed in T cells convert MHC class I peptide ligands into T cell activation receptors: a potential tool for specific targeting of pathogenic CD8… [cited by third party]