Mark Cobbold

2019037, Dec 12, 2019

May 5, 2017

16/098634

- Charlottesville VA, US
- Birmingham, GB
Paisley Trantham Myers - Charlottesville VA, US
Mark Cobbold - Winchester MA, US
Nico Büttner - Schallstadt, DE
Stacy Alyse Malaker - Oakland CA, US
Sarah Penny - Birmingham, GB

University of Virginia Patent Foundation - Charlottesville VA
The University of Birmingham - Birmingham

A61K 39/00
C12N 5/0784
C12N 5/0783
C07K 16/28
A61P 35/00
A61K 35/17
A61K 39/39
G01N 33/574
C07K 14/74
C07K 14/33

A set of target peptides are presented by HLA class I molecules on the surface of hepatocellular carcinoma (HCC) ceils and/or esophageal cancer cells. They are envisioned to among other things (a) stimulate an immune response to the proliferative disease, e.g., HCC and/or esophageal cancer, (b) function as immunotherapeutics in adoptive T-cell therapy or as a vaccine, (c) facilitate antibody recognition of tumor boundaries in surgical pathology samples, (d) act as biomarkers for early detection and/or diagnosis of the disease, and (e) act as targets in the generation anti-body-like molecules which recognize the target-peptide/MHC complex.

2021013, May 13, 2021

Jan 10, 2018

16/476628

- Boston MA, US
Matthew FRIGAULT - Somerville MA, US
Mark COBBOLD - Winchester MA, US

A61K 35/17
C12N 5/0783
C07K 14/005

The technology described herein relates to modified T cells and their use in immunotherapeutic methods. In various examples, the T cells are modified so as to decrease or eliminate OD3ζ, TRAC, and/or TRBC expression.

2017015, Jun 1, 2017

Nov 18, 2016

15/355511

- London, GB
Mark COBBOLD - Winchester MA, US

Revitope Limited - London

C07K 16/28
C07K 16/18

A targeted T-cell engaging agent for treating a condition characterized by the presence of unwanted cells includes (a) a targeting moiety that is capable of targeting the unwanted cells; (b) a first T-cell engaging domain capable of T-cell engaging activity when binding a second T-cell engaging domain, wherein the second T-cell engaging domain is not part of the agent; (c) at least one inert binding partner capable of binding to the first T-cell engaging domain such that the first T-cell engaging domain does not bind to the second T-cell engaging domain unless the inert binding partner is removed; and (d) at least one cleavage site separating the first T-cell engaging domain and the inert binding partner, wherein the cleavage site is: (i) cleaved by an enzyme expressed by the unwanted cells; (ii) cleaved through a pH-sensitive cleavage reaction inside the unwanted cell; (iii) cleaved by a complement-dependent cleavage reaction; or (iv) cleaved by a protease that is colocalized to the unwanted cell by a targeting moiety that is the same or different from the targeting moiety in the agent.

2021015, May 27, 2021

Jun 15, 2020

16/901277

- Charlottesville VA, US
- Birmingham, GB
Jennifer G. Abelin - Sommers CT, US
Mark Cobbold - Winchester MA, US
Sarah Penny - Birmingham, GB

The University of Birmingham - Birmingham

A61K 39/00
G01N 33/574

A set of target peptides are presented by HLA A*0201, B*0301, B*0702 and B*2705 on the surface of disease cells. They are envisioned to, among other things, stimulate an immune response to the proliferative disease, e.g., colorectal cancer, to function as immunotherapeutics in adoptive T cell therapy or as a vaccine, facilitate antibody recognition of tumor boundaries in surgical pathology samples, act as biomarkers for early detection and/or diagnosis of the disease, and/or act as targets in the generation antibody-like molecules which recognize the target-peptide/MHC complex.

2023002, Jan 26, 2023

Feb 8, 2021

17/170044

- Charlottesville VA, US
- Birmingham, GB
Stacy Alyse Malaker - Menlo Park CA, US
Victor H. Engelhard - Crozet VA, US
Angela L. Ambakhutwala - Glen Allen VA, US
Kara L. Cummings - Charlottesville VA, US
Rebecca C. Obeng - Charlottesville VA, US
Mark Cobbold - Winchester MA, US

University of Virginia Patent Foundation - Charlottesville VA
The University of Birmingham - Birmingham

A61K 39/00
A61K 35/15
A61K 35/17
A61K 45/06
C07K 16/28
G01N 33/574
G01N 33/68

A set of target peptides are presented by HLA A*0101, A*0201, A*0301, B*4402, B*2705, B*1402, and B*0702 on the surface of disease cells. They are envisioned to among other things (a) stimulate an immune response to the proliferative disease, e.g., cancer, (b) to function as immunotherapeutics in adoptive T cell therapy or as a vaccine, (c) facilitate antibody recognition of tumor boundaries in surgical pathology samples, (d) act as biomarkers for early detection and/or diagnosis of the disease, and (e) act as targets in the generation antibody-like molecules which recognize the target-peptide/MHC complex.

2017033, Nov 23, 2017

Dec 22, 2016

15/388896

- Charlottesville VA, US
- Birmingham, GB
Stacy Alyse Malaker - Charlottesville VA, US
Victor H. Engelhard - Crozet VA, US
Angela Zarling - Richmond VA, US
Kara L. Cummings - Charlottesville VA, US
Rebecca C. Obeng - Charlottesville VA, US
Mark Cobbold - Winchester MA, US

A61K 39/00
A61K 45/06
G01N 33/574
G01N 33/68
A61K 35/15
A61K 35/17
C07K 16/28

A set of target peptides are presented by HLA A*0101, A*0201, A*0301, B*4402, B*2705, B*1402, and B*0702 on the surface of disease cells. They are envisioned to among other things (a) stimulate an immune response to the proliferative disease, e.g., cancer, (b) to function as immunotherapeutics in adoptive T cell therapy or as a vaccine, (c) facilitate antibody recognition of tumor boundaries in surgical pathology samples, (d) act as biomarkers for early detection and/or diagnosis of the disease, and (e) act as targets in the generation antibody-like molecules which recognize the target-peptide/MHC complex.

2018034, Dec 6, 2018

Jun 28, 2018

16/021777

- Hertfordshire, GB
Mark COBBOLD - Winchester MA, US

Revitope Limited - Hertfordshire

C07K 16/28
C07K 16/30
C07K 16/18
A61K 38/00
A61K 39/395
A61K 39/00

A targeted T-cell engaging agent for treating a condition characterized by the presence of unwanted cells includes (a) a targeting moiety that is capable of targeting the unwanted cells; (b) a first T-cell engaging domain capable of T-cell engaging activity when binding a second T-cell engaging domain, wherein the second T-cell engaging domain is not part of the agent; (c) at least one inert binding partner capable of binding to the first T-cell engaging domain such that the first T-cell engaging domain does not bind to the second T-cell engaging domain unless the inert binding partner is removed; and (d) at least one cleavage site separating the first T-cell engaging domain and the inert binding partner, wherein the cleavage site is: (i) cleaved by an enzyme expressed by the unwanted cells; (ii) cleaved through a pH-sensitive cleavage reaction inside the unwanted cell; (iii) cleaved by a complement-dependent cleavage reaction; or (iv) cleaved by a protease that is colocalized to the unwanted cell by a targeting moiety that is the same or different from the targeting moiety in the agent.

2019033, Oct 31, 2019

Jan 10, 2018

16/476588

- Boston MA, US
Mark COBBOLD - Winchester MA, US
Irene SCARFO - Cambridge MA, US

C07K 14/725
C07K 16/28
C07K 14/705
C12N 5/0783
A61P 35/00
A61P 37/06
A61K 35/17
A61P 35/02

Described herein are methods for producing and utilizing an alternative signal 1 domain to construct an optimally signaling CAR. Alternative signal 1 domains of the present technology are based on alternatives to CD3ζ, including mutated ITAMs from CD3ζ (which contains 3 IT AM motifs), truncations of CD3ζ, and alternative splice variants known as CD3s, CD3 theta, and artificial constructs engineered to express fusions between CD3s or CD30 and CD3ζ. CAR polypeptides comprising alternative signal 1 domains are utilized to engineer CAR T cells. Further, this technology related to methods of treating cancer by administering to a subject in need thereof CAR T cells comprising alternative signal 1 domains.