Peptides and combination of peptides for use in immunotherapy against esophageal cancer and other cancers
Inventors
MAHR, Andrea • Weinschenk, Toni • SONG, Colette • Schoor, Oliver • FRITSCHE, Jens • Singh, Harpreet
Assignees
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Publication Number
US-12297254-B2
Publication Date
2025-05-13
Expiration Date
Abstract
The present invention relates to peptides, proteins, nucleic acids and cells for use in immunotherapeutic methods. In particular, the present invention relates to the immunotherapy of cancer. The present invention furthermore relates to tumor-associated T-cell peptide epitopes, alone or in combination with other tumor-associated peptides that can for example serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses, or to stimulate T cells ex vivo and transfer into patients. Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such, can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.
Core Innovation
The invention relates to tumor-associated T-cell peptide epitopes derived from HLA molecules, including peptide variants and elongations with flanking residues up to +4 residues per flank, and peptides consisting essentially of defined amino acid sequences. It includes peptides such as GLAPNTPGKA (SEQ ID NO: 57), provided in pharmaceutically acceptable salt forms, and scope for peptide lengths and forms for MHC class I and MHC class II binding and T-cell immunogenicity.
The disclosure further includes modification concepts for epitope peptides, including non-peptide/retro-inverso bonds, terminal chemical groups, D-isomers, and non-natural residues, and optional fusion to an invariant chain (Ii) or antibodies to enhance delivery. It also describes peptideMHC targeting by antibodies and soluble/engineered T-cell receptors, and peptide sets with large enumerated sequence coverage (SEQ ID NO: 193) in pharmaceutically acceptable salt forms and consisting essentially of peptide compositions.
The document describes identifying tumor-associated MHC peptides (TUMAPs) by HLA ligand mass spectrometry with RNASeq correlation using the XPRESIDENTae v2.1 presentation profiling pipeline. It also states that peptides are naturally presented on primary esophageal cancer and drive CD8+ responses, and frames peptide and gene over-presentation as biomarker targets across multiple cancers with emphasis on esophageal cancer.
Claims Coverage
The independent claims identified in the provided claim set are 1, 16, and 20. Across these claims, the coverage is focused on GLAPNTPGKA (SEQ ID NO: 57) and its presentation as pharmaceutically acceptable salt forms, including a pegylated version and a pharmaceutical composition context for the pegylated peptide and/or non-pegylated peptide.
A specific peptide sequence in pharmaceutically acceptable salt form
A peptide consisting of the amino acid sequence GLAPNTPGKA (SEQ ID NO: 57) in the form of a pharmaceutically acceptable salt.
A pegylated peptide sequence in pharmaceutically acceptable salt form
A pegylated peptide consisting of the amino acid sequence of GLAPNTPGKA (SEQ ID NO: 57) or a pharmaceutically acceptable salt thereof.
A specific peptide sequence in salt form
A peptide consisting of the amino acid sequence GLAPNTPGKA (SEQ ID NO: 57) in the form of a salt.
The claim coverage is directed to GLAPNTPGKA (SEQ ID NO: 57) peptides, including the peptide as a pharmaceutically acceptable salt, a pegylated version of the peptide with pharmaceutically acceptable salt options, and the peptide sequence in salt form, with the pegylated and/or non-pegylated variants further associated with pharmaceutical compositions including a pharmaceutically acceptable carrier.
Stated Advantages
Not explicitly described in patent.
Documented Applications
Peptide presentation and use in connection with human MHC class I/II binding and T-cell immunogenicity, including drive of CD8+ responses and natural presentation on primary esophageal cancer.
Identification of tumor-associated MHC peptides (TUMAPs) using HLA ligand mass spectrometry with RNASeq correlation using XPRESIDENT® v2.1.
Vaccine compositions and stimulation of T cells, including ex vivo activation and transfer of T cells.
Peptide-MHC targeting by antibodies and soluble/engineered T-cell receptors.
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