Novel chimeric antigen receptor

A technology of chimeric antigen receptors and receptors, which is applied in the field of biomedicine and can solve problems such as poor amplification ability

Pending Publication Date: 2022-07-08
CURE GENETICS CO LTD
View PDF0 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, due to the heterogeneous environment and other reasons, the expansion ability of CART (for example, universal CART) is not strong, which becomes an obstacle to further exert the curative effect of CART therapy

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Novel chimeric antigen receptor
  • Novel chimeric antigen receptor
  • Novel chimeric antigen receptor

Examples

Experimental program
Comparison scheme
Effect test

Embodiment approach

[0248] CLAIMS 1. A modified chimeric antigen receptor comprising at least one intracellular domain derived from a cytokine receptor.

[0249] 2. The modified chimeric antigen receptor of embodiment 1, wherein the intracellular domain is located in the intracellular portion of the modified chimeric antigen receptor.

[0250] 3. The modified chimeric antigen receptor of any one of embodiments 1-2, wherein the cytokine receptor comprises IL7RA, IL15RA, IL9R, IL3RA, IL21R and / or IL23R.

[0251] 4. The modified chimeric antigen receptor of any one of embodiments 1-3, wherein the cytokine receptor comprises IL7RA.

[0252] 5. The modified chimeric antigen receptor of any one of embodiments 1-4, wherein the cytokine receptor comprises IL21R.

[0253] 6. The modified chimeric antigen receptor of any one of embodiments 1-5, comprising a costimulatory domain.

[0254] 7. The modified chimeric antigen receptor of embodiment 6, wherein the costimulatory domain comprises a costimulatory ...

Embodiment 1

[0348] Example 1 Construction of a novel CAR structure

[0349] 1.1 Construction of BBz-ILR and 28z-ILR structures

[0350] 1.1.1 Nucleic acid sequences for synthesizing BBz and 28z

[0351] The nucleic acid sequences of BBz (SEQ ID NO: 1) and 28z (SEQ ID NO: 2) were obtained by gene synthesis. The corresponding amino acid sequences are BBz: SEQ ID NO:3, 28z: SEQ ID NO:4.

[0352] 1.1.2 Connect the nucleic acid sequences of BBz and 28z to the lentiviral vector pELPs

[0353] The BBz or 28z were ligated into the lentiviral vector pELPs (SEQ ID NO: 5) by restriction endonuclease BamHI digestion.

[0354] 1.1.3 Synthesis of ILR Sequence Fragments

[0355]The nucleic acid sequence of the truncated fragment (IL2RB-F) of the synthetic IL2RB intracellular domain (as shown in SEQ ID NO: 6, the amino acid sequence as shown in SEQ ID NO: 7), the nucleic acid sequence of YRHQ in BBz (SEQ ID NO: 61), the nucleic acid sequence (SEQ ID NO: 62) of YRHQ in 28z, the nucleic acid sequence ...

Embodiment 2

[0389] Example 2 Preparation of lentivirus with recombinant vector

[0390] 2.1 Extraction of recombinant vector

[0391] The pELPs-BBz, pELPs-28z, pELPs-BBz-ILC, pELPs-28z-ILC, pELPs-BBz-IL1 to 8 and pELPs-28z-IL1 to 8 recombinant vectors constructed above were retransformed into E. coli. Pick a single clone from the transformed plate and put it into a shaker tube of 3ml of liquid LB medium containing ampicillin, rotate at 220rpm, and cultivate with shaking on a shaker for 8h; draw 500μl from the activated bacterial solution and inoculate it into 250ml of ammonia-containing liquid In the liquid LB medium of penicillin, 220rpm, shaker for 12-16h. Recombinant vector extraction was performed using Qiagen HiSpeed ​​Plasmid Maxi Kit (Cat. No. 12662) according to the experimental procedure provided by the kit. After extracting the recombinant vector, Nanodrop (Thermo Fisher Scientific) was used to detect the concentration of the recombinant vector, and the content of the recombin...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

No PUM Login to view more

Abstract

The present application relates to a novel chimeric antigen receptor comprising at least one intracellular domain selected from a receptor of a cytokine or a variant thereof. The invention also relates to an immune cell containing the novel chimeric antigen receptor structure. In addition, the invention also relates to a method for enhancing the amplification capacity of the immune cell containing the novel chimeric antigen receptor structure and a method for enhancing a signal of a JAK-STAT signal channel in the immune cell containing the novel chimeric antigen receptor structure.

Description

technical field [0001] The present application relates to the field of biomedicine, in particular to a novel chimeric antigen receptor. Background technique [0002] At present, chimeric antigen receptor-engineered Tcell therapy (CART) is an effective adoptive cellular immunotherapy. Effector T lymphocytes produce targeted cytotoxicity against tumor cells to achieve the purpose of eliminating tumor cells in vivo. [0003] Chimeric antigen receptors (CARs) include an extracellular antigen recognition domain, a transmembrane domain, a costimulatory domain and an intracellular signaling domain. CAR redirects the specificity of immune effector cells and triggers proliferation, cytokine production, and can also mediate target antigen-expressing cell death in a major histocompatibility (MHC)-independent manner. [0004] In recent years, CAR-modified T cell technology has shown good anti-tumor effects in the treatment of leukemia, lymphoma and other malignant tumors. However, du...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(China)
IPC IPC(8): C07K19/00
CPCC07K16/2803C07K14/7051C07K2319/02C07K2319/03C07K2319/33C07K2319/74
Inventor 贾璐盈林彦妮袁慧方姣龙
Owner CURE GENETICS CO LTD
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products