Disclosed herein include a natural killer (NK) cell genetically modified to comprise a recombinant nucleic acid encoding C-X-C Motif Chemokine Receptor 1 (CXCR1), a pharmaceutical composition comprising the NK cell, methods of preparing the NK cell, and method of treating cancer or tumor using the NK cell.

Provided herein are compositions and methods for manufacturing engineered lymphocytes. Also provided are the prepared engineered lymphocytes which have increased proportions of juvenile/naive lymphocytes leading to increased therapeutic efficacy. The methods in various embodiments are expedited as compared to the conventional technology, and produce lymphocytes with improved viability, transduction success rates, and in vivo antitumor efficacy.

Provided herein are acute myeloid leukemia antigen targets for chimeric receptors and methods of using same.

Provided are methods and compositions for obtaining functionally enhanced derivative effector cells obtained from directed differentiation of genomically engineered iPSCs. The iPSC-derived effector cells provided herein have stable and functional genome editing that delivers improved or enhanced therapeutic effects. Also provided are therapeutic compositions and the use thereof comprising the functionally enhanced derivative effector cells alone, or with antibodies or checkpoint inhibitors in combination therapies.

Provided herein are T-cell receptors (TCRs) that when expressed recombinantly on the surface of a T cell are able to recognize the MAGE-B2-derived peptide GVYDGEEHSV (SEQ ID NO: 1) when presented by HLA-A*02:01 sufficiently to activate the recombinant T cell. Certain TCRs provided herein also are able to recognize the MAGE-A4-derived peptide GVYDGREHTV (SEQ ID NO:2) sufficiently to activate the recombinant T cell. Importantly, exemplary TCRs provided herein were thoroughly screened for lack of cross-reactivity with similar peptides that may be presented by normal cells or tissue and for alloreactivity.

Described herein are immunoresponsive cells which are useful for their preventive and therapeutic potential against autoimmune diseases and rejections of solid organ transplants.

Provided herein are antibodies that specifically target integrin beta-2 and compositions comprising such antibodies for therapeutic and diagnostic applications. The antibodies comprise an integrin beta-2 binding domain comprising a heavy chain variable region comprising an HCDR1 sequence comprising ISYYYM, an HCDR2 sequence comprising SISSSSGYTY; and an HCDR3 sequence comprising GAM; and a light chain variable region comprising an LCDR1 sequence comprising SVSSA, an LCDR2 sequence comprising SASSLYS; and an LCDR3 sequence comprising FSSGSWAPI.

Compounds that either produced a higher proportion or greater absolute number of phenotypically identified naive, stem cell memory, central memory T cells, adaptive NK cells, and type I NKT cells are identified. Compositions and methods for modulating immune cells including T, NK, and NKT cells for adoptive cell therapies with improved efficacy are provided.

The present disclosure generally relates to, inter alia, a new class of receptors engineered to modulate transcriptional regulation in a ligand-dependent manner. Particularly, the new receptors, even though derived from Notch, do not require the Notch negative regulatory regions previously believed to be essential for the functioning of the receptors. In addition, the new receptors described herein incorporate an extracellular oligomerization domain to promote oligomer formation of the chimeric receptors. The disclosure also provides compositions and methods useful for producing such receptors, nucleic acids encoding same, host cells genetically modified with the nucleic acids, as well as methods for modulating an activity of a cell and/or for the treatment of various health conditions such as cancers.

Provided are an anti-Claudin 18.2 antigen-binding fragment or antibody, and the use thereof. CDR3 of a heavy chain variable region of the antigen-binding fragment comprises an amino acid sequence shown in SEQ ID NO. 3. CDR3 of a light chain variable region of the antigen-binding fragment comprises an amino acid sequence shown in SEQ ID NO. 6. The provided antigen-binding fragment and anti-Claudin 18.2 antibody can specifically bind to a variety of sources of Claudin 18.2 proteins, have no binding effect on other proteins, and have a high specificity. In addition, a chimeric antigen receptor and a CAR-T cell prepared by means of the antibody have obvious cytotoxicity on cells stably expressing the Claudin 18.2 protein.