Disclosed herein are compositions related to conjugated polypeptides with MTA/ADO-degrading enzyme activity. The conjugated polypeptides are engineered to allow for maximal conjugation while maintaining catalytic activities. Also disclosed are nucleic acids, expression vectors, and host cells related to the conjugated polypeptides. Further disclosed are methods of using the pharmaceutical formulations comprising above to treat cancer.

Methods and compositions related to the engineering of a protein with MTA/ADO-degrading enzyme activity are described. For example, in certain aspects there may be disclosed an MTase capable of degrading MTA/ADO. Furthermore, certain aspects of the invention provide compositions and methods for the treatment of cancer or SCID with an MTase using the disclosed proteins or nucleic acids.

The present invention relates to the field of modified proteins, immunogenic compositions and vaccines comprising the modified proteins, their manufacture and the use of such compositions in medicine. More particularly, it relates to a modified EPA (Exotoxin A of Pseudomonas aeruginosa) protein. The modified EPA can be used as a carrier protein for other antigens, particularly saccharide antigens or other antigens lacking T cell epitopes.

The present disclosure provides modified looped proteins comprising at least one looped region, wherein the at least one looped region comprises a cell penetrating peptide (CPP). In some embodiments, the present disclosure provides polynucleotides encoding the modified looped proteins and methods for their production.

A genetically engineered bacterium includes a genome of the Eschericia coli and a mutant encoding gene hisG* of a Corynebacterium glutamicum ATP phosphoribosyl transferase HisG on the genome, and the gene hisG* is strongly expressed to enhance activity of a key enzyme HisG for histidine synthesis. The gene hisG* has a nucleotide sequence as shown in SEQ ID NO: 1; a copy number of histidine operon genes hisDBCHAFI of the Eschericia coli is further increased on the genome to enhance a terminal synthetic route of histidine; an encoding gene lysE from an arginine/lysine transportprotein of the Corynebacterium glutamicum is further integrated to the genome and strongly expressed to promote the intracellular histidine secrete to the extracellular space; and an encoding gene rocG of glutamate dehydrogenase of Bacillus subtilis is further integrated to the genome and strongly expressed to promote generation of histidine.

A genetically engineered bacterium includes a genome of the Eschericia coli and a mutant encoding gene hisG* of a Corynebacterium glutamicum ATP phosphoribosyl transferase HisG on the genome, and the gene hisG* is strongly expressed to enhance activity of a key enzyme HisG for histidine synthesis. The gene hisG* has a nucleotide sequence as shown in SEQ ID NO: 1; a copy number of histidine operon genes hisDBCHAFI of the Eschericia coli is further increased on the genome to enhance a terminal synthetic route of histidine; an encoding gene lysE from an arginine/lysine transportprotein of the Corynebacterium glutamicum is further integrated to the genome and strongly expressed to promote the intracellular histidine secrete to the extracellular space; and an encoding gene rocG of glutamate dehydrogenase of Bacillus subtilis is further integrated to the genome and strongly expressed to promote generation of histidine.

In one aspect, the present invention jointly expresses SOD and NAMPT proteins. The activity of SOD and NAMPT expressed by silkworm pupae inoculated with viruses is higher than that of silkworm pupae that are not inoculated with viruses, which proves that it is feasible to jointly express SOD and NAMPT with silkworms. It is expected to prepare an effective anti-aging drug.

Mutant mono ADP-ribose-polymerases (mono-PARP) proteins and small molecule compound substrates specific for the mutant mono-PARP proteins as well as methods of using these compositions to identify protein targets of the mono-PARPs and to screen for antagonists of the mono-PARPs are described.

The present invention relates to an enzyme-catalyzed process for producing UDP-galactose from low-cost substrates uridine monophosphate and D-galactose in a single reaction mixture. Said process can be operated (semi)continuously or in batch mode. Said process can be extended to uridine as starting material instead of uridine monophosphate. Further, said process can be adapted to produce galactosylated molecules and biomolecules including saccharides, proteins, peptides, glycoproteins or glycopeptides, particularly human milk oligosaccharides (HMO) and (monoclonal) antibodies.

Disclosed are a construction method of a recombinant drug-resistant Mycobacterium bovis (M. bovis) Bacillus Calmette-Guerin (BCG) strain and a pharmaceutical composition for treating tuberculosis (TB). The construction method includes: using BCG as an original bacterial strain to construct a drug-resistant BCG strain resistant to at least one selected from the group consisting of STR, LFX, EMB, PRO, PAS, and AMK; and further inserting sequence fragments that can express related antigens Ag85b and Rv2628 causing an immune response into a genome of the strain to construct a recombinant drug-resistant BCG strain. The recombinant drug-resistant BCG strain can compete with Mycobacterium tuberculosis (Mtb) for growth, thereby accelerating the death of Mtb. When used in combination with a drug for treating TB, the recombinant drug-resistant BCG strain can further enhance a therapeutic effect for Mtb, and can also avoid re-infection of a patient.