79 results about "Peptide specificity" patented technology

A new method to capture, purify and expand antigen-specific T lymphocytes has been developed using magnetic beads coated with recombinant MHC class I molecules. This method was optimized using homogenous populations of naive T cells purified from mice transgenic for the 2C T cell receptor (TCR). These T cells were captured on beads coated with MHC class I molecules and the relevant antigenic peptides. MHC and peptide specificity was confirmed by the usage of irrelevant MHC peptide combinations. An enrichment of 800 to 1600 fold was measured, using 2C T cells mixed with irrelevant T cells, starting from a 2C T cell frequency of 1/3000. The same approach was used to purify antigen-specific CD8⁺ T cells from total CD8⁺ T cells from naive mice. The recovered cells could be expanded and specifically kill target cells in vitro; they had a significant effect in vivo as well. We expect this procedure to be suitable to purify and expand in vitro tumor- and virus-specific killer T cells for use in cell therapy.

Human myelin basic protein (h-MBP) has a molecular weight of 18.5 KD and contains 170 amino acid residues. Synthetic peptides ranging in length from about 8 to 25 residues and covering the entire length of the protein have been produced. Antibodies to h-MBP (anti-MBP) were found to be neutralized by the synthetic peptides, in vitro, which span the h-MBP from about amino acid residue 61 to about amino acid residue 106. The peptides, which cover both the amino (about residues 1 to 63) and carboxy (about residues 117 to 162) terminals of h-MBP did not neutralize purified anti-MBP. Intrathecal administratin of peptide MBP(75-95), MBP(86-95), or MBP(82-98) produced complete binding-neutralization of free (F) anti-MBP with no change in bound (B) levels. A control peptide MBP35-58 had no effect on F or B anti-MBP levels. Intravenous administration of MBP(75-95), MBP(86-95), or MBP(82-98) resulted in significant decline of F and B CSF anti-MBP levels. Administration of MBP synthetic peptides to MS patients either intrathecally or intravenously did not have any adverse neurological effects and systemic complications did not occur. The MBP epitope for MS anti-MBP has been localized to an area between amino acid 86 and amino acid 95.

A cell culture microcarrier includes (1) a polystyrene microcarrier base having a remnant of a carboxylic acid group, and (ii) a polypeptide conjugated to the base via the remnant of the carboxylic acid group. The polypeptide may contain a cell adhesive sequence, such as RGD. Cells cultured with such microcarriers exhibit peptide-specific binding to the microcarriers.

The invention discloses 347 novel phosphorylation sites identified in carcinoma, peptides (including AQUA peptides) comprising a phosphorylation site of the invention, antibodies specifically bind to a novel phosphorylation site of the invention, and diagnostic and therapeutic uses of the above.

The invention discloses 322 novel acetylation sites identified in various cancers, peptides (including AQUA peptides) comprising a acetylation site of the invention, antibodies specifically bind to a novel acetylation site of the invention, and diagnostic and therapeutic uses of the above.

A new method to capture, purify and expand antigen-specific T lymphocytes has been developed using magnetic beads coated with recombinant MHC class I molecules. This method was optimized using homogenous populations of naive T cells purified from mice transgenic for the 2C T cell receptor (TCR). These T cells were captured on beads coated with MHC class I molecules and the relevant antigenic peptides. MHC and peptide specificity was confirmed by the usage of irrelevant MHC peptide combinations. An enrichment of 800 to 1600 fold was measured, using 2C T cells mixed with irrelevant T cells, starting from a 2C T cell frequency of {fraction (1/3000)}. The same approach was used to purify antigen-specific CD8+ T cells from total CD8+ T cells from naive mice. The recovered cells could be expanded and specifically kill target cells in vitro; they had a significant effect in vivo as well. We expect this procedure to be suitable to purify and expand in vitro tumor- and virus-specific killer T cells for use in cell therapy.

The invention discloses 332 novel acetylation sites identified in various cancers, peptides (including AQUA peptides) comprising a acetylation site of the invention, antibodies specifically bind to a novel acetylation site of the invention, and diagnostic and therapeutic uses of the above.

The invention describes peptide ligands specific for human plasma Kallikrein.

Cytotoxic αβ T cells form an essential component in immunity to infections and tumors, and are also implicated in host defense against these challenges. The present disclosure demonstrates the ability of activated γδ T cells to cross-present exogenous antigens to CD8⁺αβ T cells, a process previously thought to be mediated best by dendritic cells. In particular, the present disclosure provides a method for cross-presentation of antigen derived from tumor cell or microbial organisms such as viruses, bacteria, yeasts, parasites, and the like, or from cells infected with such organisms, to a CD8⁺αβ T cell. Still further, the present disclosure provides a method for treatment of a tumor or a chronic or recurrent infectious disease, comprising delivering an antigen-presenting autologous γδ T cell population above into a patient requiring such treatment. Still yet further, a method is described for preparing a peptide-specific effector T cell.

The present invention provides a monoclonal antibody recognizing modification after translation of p53 in a manner specific to a modification site, an antibody microarray comprising the antibody immobilized on a substrate, etc. Disclosed is a monoclonal antibody which reacts specifically with a peptide consisting of an amino acid sequence of at least 6 consecutive amino acids containing a predetermined amino acid residue of the amino acid sequence represented by SEQ ID NO: 1, wherein the amino acid residue is phosphorylated or acetylated, or with a peptide having one to several arbitrary amino acids added to the above peptide, but does not react with the above peptide which is not phosphorylated or acetylated.

The invention discloses a T cell receptor for recognizing an EBV antigen and application of the T cell receptor. The T cell receptor (TCR) comprises an alpha chain containing a variable region and/or a beta chain containing a variable region, wherein the variable region of the alpha chain comprises a complementarity determining region 3 (CDR3) containing an amino acid sequence of AVVNNNDMR (SEQ ID NO: 3); and/or the variable region of the beta chain comprises a complementarity determining region 3 (CDR3) comprising ASSPGRWYEQY (SEQ ID NO: 6). The TCR provided by the invention can be specifically combined with an EBV antigen short peptide, and T cells transducing the TCR can be specifically activated and have a very strong killing effect on target cells.

The invention discloses novel phosphorylation sites identified in carcinoma and/or leukemia, peptides (including AQUA peptides) comprising a phosphorylation site of the invention, antibodies specifically bind to a novel phosphorylation site of the invention, and diagnostic and therapeutic uses of the above.

The invention relates to pharmaceutical compositions that contain COVID-19 peptide specific cytotoxic T cells, and to methods for treating or preventing COVID-19 infection.

The present invention provides nonamer peptides derived from fibroblast activation protein α (FAPα) for the treatment of solid tumors. These peptides specifically bind to HLA, defined by an IC₅₀ value of less than about 50 μM, induce a T cell response in a subject, wherein position No. 2 of said nonamer peptide is leucine (L), isoleucine (I) or methionine (M), and position No. 9 of said nonamer peptide is leucine (L), valine (V) or isoleucine (I). Further, a composition comprising a nonamer peptide and methods for the prophylactic and therapeutic treatment are provided.