C07K2319/73

STABILIZED MINIMAL COILED-COIL MIMETICS
20210277059 · 2021-09-09 ·

This invention relates to a macrostructure that includes an antiparallel coiled-coil structure shown below or a parallel coiled-coil structure shown below and described in the present application.

METHOD FOR THE PRODUCTION OF BI-FUNCTIONAL CELLS TO TREAT NEOPLASIA

Method for the production of bi-functional cells comprising engineering a starting cell population with a phenotype attributable to human pericytes extracted from adipose tissue (AD-PC), obtaining engineered cells, known as bi-functional AD-PCs, expressing (which means that they produce) simultaneously both the anti-tumor molecule TRAIL and also the truncated form of a chimeric receptor targeted against the GD2 antigen (GD2 tCAR); this dual targeting (understood as reaching a specific target), based on affinity and mediated by both TRAIL and also GD2 tCAR, supports the prediction of combining site-specificity with a prolonged retention of AD-PCs in tumors expressing the antigen GD2, so as to achieve a more effective release of TRAIL for still incurable tumors.

SYNTHEKINE COMPOSITIONS AND METHODS OF USE
20210260162 · 2021-08-26 ·

Engineered synthekines and methods of use thereof are provided.

Coiled-coil connector

A connector of a helical coiled coil-type structure connecting a first and a second molecule, wherein the first molecule comprises a peptidic first alpha-helix and the second molecule comprises a peptidic second alpha-helix, which second alpha-helix is coiled to the first alpha-helix. The first alpha-helix comprises a C-terminal region consisting of a repeat of an amino acid motif a-x.sub.1 and the C-terminal motif a-x.sub.1-x.sub.2, or an N-terminal region consisting of a repeat of an amino acid motif x.sub.1-a and the N-terminal motif x.sub.2-x.sub.1-a, where a is a motif sequence of 4-8 amino acids, x.sub.1 is Lysine, and x.sub.2 is an extension of the motif. The extension consists of 1-10 amino acids and does not comprise more than 4 consecutive amino acids incorporated in said motif a-x.sub.1 or x.sub.1-a. In a multimeric protein, two polypeptide chains can be connected to each other by such connector.

NOVEL MAMMALIAN EXPRESSED HUMAN IMMUNODEFICIENCY VIRUS ENVELOPE PROTEIN ANTIGENS

Novel mammalian expressed human immunodeficiency virus envelope Protein antigens Various embodiments of the invention relate to polypeptides comprising 1-10 or more epitopes of the HIV envelope protein and a fusion protein, wherein the polypeptide lacks the transmembrane domain of the HIV gp41 protein. Such polypeptides may be expressed in mammalian cells, such as human cells, to produce, for example, polypeptides that are useful in developing novel anti-HIV antibodies. Polypeptides described herein and novel antibodies developed therefrom are generally useful for medical diagnostics, and they may also be useful in the prophylactic and therapeutic treatment of HIV.

Bispecific CD16-Binding Molecules and Their Use in the Treatment of Disease

The present invention is directed to molecules (e.g., an antibody, a diabody, an scFv, an antibody, a TandAb, etc.) capable of binding an epitope of human CD16 (a “CD16 Binding Molecule”). The present invention is further directed to CD 16 Binding Molecules that are capable of binding an epitope of human CD16 and one or more epitope(s) of a Disease Antigen (“DA”) (e.g., a “CD16 x DA Binding Molecule”). The present invention is particularly directed to such CD16 x DA Binding Molecules that are antibodies, or that comprise an Epitope Binding Domain thereof, or are diabodies (including DART® diabodies), bispecific antibodies, TandAbs, other multispecific binding molecules (e.g., trivalent TRIDENT™ molecules), etc. The invention particularly concerns CD16 x DA Binding Molecules that are capable of binding a Disease Antigen that is a Cancer Antigen or a Pathogen-Associated Antigen in addition to being able to bind CD 16. The invention particularly concerns the use of such CD16 and CD16 x DA Binding Molecules in the treatment of cancer and pathogen-associated diseases. The present invention is also directed to pharmaceutical compositions that comprise such molecule(s).

LEUCINE ZIPPER-BASED COMPOSITIONS AND METHODS OF USE

The presently disclosed subject matter provides compositions and systems for cell-based immunotherapy. In certain non-limiting embodiments, the system comprises a membrane-bound polypeptide and at least one soluble polypeptide that is capable of dimerizing with the membrane-bound polypeptide.

CELL SORTING SYSTEMS AND METHODS OF USE

The presently disclosed subject matter provides methods and systems for isolating cells expressing specific constructs. In certain non-limiting embodiments, the system comprises a membrane-bound polypeptide and a soluble polypeptide that is capable of dimerizing with the membrane-bound polypeptide.

Recombinant metapneumovirus F proteins and their use

Metapneumovirus (MPV) F proteins stabilized in a prefusion conformation, nucleic acid molecules and vectors encoding these proteins, and methods of their use and production are disclosed. In several embodiments, the MPV F proteins and/or nucleic acid molecules can be used to generate an immune response to MPV in a subject. In additional embodiments, the therapeutically effective amount of the MPV F ectodomain trimers and/or nucleic acid molecules can be administered to a subject in a method of treating or preventing MPV infection.

SYSTEMS AND METHODS FOR THE PREPARATION OF PEPTIDE-MHC-I COMPLEXES WITH NATIVE GLYCAN MODIFICATIONS
20210155670 · 2021-05-27 ·

Disclosed herein are novel glycosylated peptide receptive MHC-I complexes that allow for efficient production of glycosylated MHC-I multimers. Such glycosylated peptide receptive MHC-I complexes include a single-chain MHC-I construct and are produced in mammalian expression systems (e.g., CHO and HEK cells) that allow for the glycosylation of the complexes at one or more native positions. Multimers (e.g., tetramers) produced from the glycosylated peptide receptive MHC-I complexes provided herein advantageously allow for the identification of high-affinity T cell and natural killer cell receptors previously unidentified using traditional unglycosylated MHC tetramers.