Patent classifications
C12N9/90
RIBULOSE-PHOSPHATE 3-EPIMERASE MOTIF HAVING LOW SIDE REACTIVITY AND ENZYME INCLUDING THE SAME
Provided are ribulose-phosphate 3-epimerase, a microorganism and a composition, each including the ribulose-phosphate 3-epimerase, and a method of producing psicose-6-phosphate or psicose using the same.
RIBULOSE-PHOSPHATE 3-EPIMERASE MOTIF HAVING LOW SIDE REACTIVITY AND ENZYME INCLUDING THE SAME
Provided are ribulose-phosphate 3-epimerase, a microorganism and a composition, each including the ribulose-phosphate 3-epimerase, and a method of producing psicose-6-phosphate or psicose using the same.
Regulatable chimeric antigen receptor
Compositions and methods relating to regulatable chimeric antigen receptors (RCARs), where the intracellular signaling or proliferation of the RCAR can be controlled to optimize the use of an RCAR-expressing cell to provide an immune response, are provided. For example, a RCAR can comprise a dimerization switch that, upon the presence of a dimerization molecule, can couple an intracellular signaling domain to an extracellular recognition element, e.g., an antigen binding domain, an inhibitory counter ligand binding domain, or costimulatory ECD domain. An RCAR can be engineered to include an appropriate antigen binding domain that is specific to a desired antigen target and used in the treatment of a disease.
Regulatable chimeric antigen receptor
Compositions and methods relating to regulatable chimeric antigen receptors (RCARs), where the intracellular signaling or proliferation of the RCAR can be controlled to optimize the use of an RCAR-expressing cell to provide an immune response, are provided. For example, a RCAR can comprise a dimerization switch that, upon the presence of a dimerization molecule, can couple an intracellular signaling domain to an extracellular recognition element, e.g., an antigen binding domain, an inhibitory counter ligand binding domain, or costimulatory ECD domain. An RCAR can be engineered to include an appropriate antigen binding domain that is specific to a desired antigen target and used in the treatment of a disease.
PRODUCTION OF FRUCTOSE FROM OLIGO-/ AND/OR POLYSACCHARIDES
The present invention relates to a method for converting at least one oligo- and/or polysaccharide into fructose comprising the steps of: a) adding to a composition comprising water, phosphate and at least one oligo- and/or polysaccharide at least four enzymes, and b) subsequently enzymatically converting the at least one oligo- and/or polysaccharide to fructose in the presence of the at least four enzymes, wherein in step a) at least one additional saccharide is added, whereby the at least one additional saccharide is selected from the group consisting of saccharides comprising 20 or less monosaccharide residues and/or combinations thereof; wherein in step a) the at least four enzymes, preferably at least five enzymes, are selected from the group consisting of transferases, phosphorylases, mutases, isomerases, hydrolases, phosphatases and combinations thereof; and wherein at least one enzyme in step a) is a phosphatase.
PRODUCTION OF FRUCTOSE FROM OLIGO-/ AND/OR POLYSACCHARIDES
The present invention relates to a method for converting at least one oligo- and/or polysaccharide into fructose comprising the steps of: a) adding to a composition comprising water, phosphate and at least one oligo- and/or polysaccharide at least four enzymes, and b) subsequently enzymatically converting the at least one oligo- and/or polysaccharide to fructose in the presence of the at least four enzymes, wherein in step a) at least one additional saccharide is added, whereby the at least one additional saccharide is selected from the group consisting of saccharides comprising 20 or less monosaccharide residues and/or combinations thereof; wherein in step a) the at least four enzymes, preferably at least five enzymes, are selected from the group consisting of transferases, phosphorylases, mutases, isomerases, hydrolases, phosphatases and combinations thereof; and wherein at least one enzyme in step a) is a phosphatase.
RECOMBINANT INFLUENZA VIRUS-LIKE PARTICLES (VLPS) PRODUCED IN TRANSGENIC PLANTS
A method for synthesizing influenza virus-like particles (VLPs) within a plant or a portion of a plant is provided. The method involves expression of influenza HA in plants and the purification by size exclusion chromatography. The invention is also directed towards a VLP comprising influenza HA protein and plant lipids. The invention is also directed to a nucleic acid encoding influenza HA as well as vectors. The VLPs may be used to formulate influenza vaccines, or may be used to enrich existing vaccines.
RECOMBINANT INFLUENZA VIRUS-LIKE PARTICLES (VLPS) PRODUCED IN TRANSGENIC PLANTS
A method for synthesizing influenza virus-like particles (VLPs) within a plant or a portion of a plant is provided. The method involves expression of influenza HA in plants and the purification by size exclusion chromatography. The invention is also directed towards a VLP comprising influenza HA protein and plant lipids. The invention is also directed to a nucleic acid encoding influenza HA as well as vectors. The VLPs may be used to formulate influenza vaccines, or may be used to enrich existing vaccines.
PRODUCTION OF GPP AND CBGA IN A METHYLOTROPHIC YEAST STRAIN
This invention is an improved method of robust and scalable production of precursors of active cannabinoids, including geranyl pyrophosphate (GPP) and/or cannabigerolic acid (CBGA), in a methylotrophic yeast host cell. The improved methods incorporate a polypeptide encoding an Erg20 variant (F98W/N128W) into a methylotrophic yeast host cell, for example Pichia pastoris (Komagataella phaffii), that biases the natural production of FPP and GPP towards GPP, a precursor to the intermediate CBGA, crucial to the synthesis of active cannabinoids.
PRODUCTION OF GPP AND CBGA IN A METHYLOTROPHIC YEAST STRAIN
This invention is an improved method of robust and scalable production of precursors of active cannabinoids, including geranyl pyrophosphate (GPP) and/or cannabigerolic acid (CBGA), in a methylotrophic yeast host cell. The improved methods incorporate a polypeptide encoding an Erg20 variant (F98W/N128W) into a methylotrophic yeast host cell, for example Pichia pastoris (Komagataella phaffii), that biases the natural production of FPP and GPP towards GPP, a precursor to the intermediate CBGA, crucial to the synthesis of active cannabinoids.