Abstract: Provided are a novel antibiotic preparation method and platform system based on the method, belonging to a novel drug development method. The method is based on a fixed structural formula: F—R, wherein F is an effect area, and R is an identification area. At the prior art level, the present invention can quickly develop a specific novel antibiotic for most pathogenic microorganisms or biological cells. Also provided is a platform for implementing the method, ensuring that the novel antibiotic is developed in an efficient streamlined process.

Abstract: Provided are methods for highly expressing recombinant protein of engineering bacteria and the use thereof. The method comprises the following steps: (1) engineering bacteria of Escherichia coli with pET system are transfected with recombinant mutated plasmid to obtain positive monoclonal colonies; (2) the positive monoclonal colonies are enriched to obtain a seed bacteria solution, and the seed bacteria solution is induced to enrichment and growth in a large amount; and (3) the bacteria supernatant containing the recombinant protein as the expression target is separated, and then the recombinant protein in the bacteria supernatant is extracted and purified. The method is characterized in that the engineering bacteria of Escherichia coli with pET system are E. coli B834 (DE3).

Abstract: Provided are a hybridoma cell CGMCC No. 4783 that secretes a monoclonal antibody of an anti-cyanobacteria cell surface antigen, and the secreted monoclonal antibody thereof. Also provided are an anti-cyanobacteria recombinant antibody polypeptide, encoding gene, preparation method and use thereof. The anti-cyanobacteria recombinant antibody polypeptide is composed of an anti-cyanobacteria antibody mimetic polypeptide operably linearly connecting to the carboxyl terminal of an Escherichia coli polypeptide. The anti-cyanobacteria antibody mimetic polypeptide is a polypeptide with cyanobacteria identifying and binding capability designed based on an antigen binding fragment of the monoclonal antibody secreted by the CGMCC No. 4783 hybridoma cell. The anti-cyanobacteria recombinant antibody polypeptide directly form an ion channel on the cell membrane of a cyanobacteria to kill the cyanobacteria, targeted killing the cyanobacteria (prokaryote) without killing other beneficial eukaryotic cell algae.

Abstract: The present invention belongs to field of biology and medicine, and especially relates to a novel antibiotic comprising an antibody mimetic antibody, its preparation methods and uses thereof. A novel antibiotic comprising a antibody mimetic covalently bonded to the carboxyl end of a colicin polypeptide or a channel-forming domain polypeptide of a colicin, wherein said colicin is selected from the group consisting of Colicin E1, Ia, Ib, A, B, N; wherein said antibody mimetic being yielded by fusing two complementarity determining regions (CDRs), VHCDR1 and VLCDR3 through a cognate framework region (VHFR2) of an immunoglobulin; wherein said the immunoglobulin specifically recognizes the bacterial porins. Its antibacterial ability is a thousandfold powerful than normal antibiotics. Due to its unique action mechanism, drug resistance resulted in mutation can hardly be acquired by pathogenic bacteria. And the antibiotic will not hurt normal human cells when it kills pathogenic bacteria.

Abstract: Provided are a novel antibiotic preparation method and platform system based on the method, belonging to a novel drug development method. The method is based on a fixed structural formula: F—R, wherein F is an effect area, and R is an identification area. At the prior art level, the present invention can quickly develop a specific novel antibiotic for most pathogenic microorganisms or biological cells. Also provided is a platform for implementing the method, ensuring that the novel antibiotic is developed in an efficient streamlined process.

Abstract: The present invention provides a fusion polypeptide against EB virus-induced tumor, which comprises an antibody or a mimetic antibody against EB virus and an ion channel forming colicin selected form E1, Ia, Ib, A, B, N and their mutants. The present invention also provides a colicin Ia mutant, which comprises mutations of G11A, H22G, A26G, V31L, and H40D. The present invention also provides a gene, vector, preparation method and use of the fusion polypeptide, and provides a gene and use of the mutant.

Abstract: Provided are a hybridoma cell CGMCC No. 4783 that secretes a monoclonal antibody of an anti-cyanobacteria cell surface antigen, and the secreted monoclonal antibody thereof. Also provided are an anti-cyanobacteria recombinant antibody poly-peptide, encoding gene, preparation method and use thereof. The anti-cyanobacteria recombinant antibody polypeptide is composed of an anti-cyanobacteria antibody mimetic polypeptide operably linearly connecting to the carboxyl terminal of an Escherichia coli polypeptide. The anti-cyanobacteria antibody mimetic polypeptide is a polypeptide with cyanobacteria identifying and binding cap-ability designed based on an antigen binding fragment of the monoclonal antibody secreted by the CGMCC No.4783 hybridoma cell. The anti-cyanobacteria recombinant antibody polypeptide directly form an ion channel on the cell membrane of a cyanobacteria to kill the cyanobacteria, targeted killing the cyanobacteria (prokaryote) without killing other beneficial eukaryotic cell algae.

Abstract: The present invention belongs to field of biology and medicine, and especially relates to a novel antibiotic, its nucleotide sequence, methods of construction and uses thereof. A novel antibiotic, wherein the end of any peptide of the allosteric colicin is connected linearly to the end of peptide of the Staphylococcus aureus pheromone AgrD I, AgrD II, AgrD III, AgrD IV or Staphylococcus epidermidis pheromone. Wherein the allosteric colicin being yielded by artificially mutating the amino acid residues G11A, H22R, A26G, V31L and H40K in the peptide chain of wild type Colicin E1, Ia, Ib, A, B, N, or their ion channel-forming structural domain. In comparison with the traditional antibiotics, the novel antibiotics in the present invention are not likely to lead to drug resistance and cause hypersensitivity reaction.

Abstract: The present invention provides a fusion polypeptide against EB virus-induced tumor, which comprises an antibody or a mimetic antibody against EB virus and an ion channel forming colicin selected form E1, Ia, Ib, A, B, N and their mutants. The present invention also provides a colicin Ia mutant, which comprises mutations of G11A, H22G, A26G, V31L, and H40D. The present invention also provides a gene, vector, preparation method and use of the fusion polypeptide, and provides a gene and use of the mutant.

Abstract: The present invention belongs to field of biology and medicine, and especially relates to a novel antibiotic, its nucleotide sequence, methods of construction and uses thereof. A novel antibiotic, wherein the end of any peptide of the allosteric colicin is connected linearly to the end of peptide of the Staphylococcus aureus pheromone AgrD I, AgrD II, AgrD III, AgrD IV or Staphylococcus epidermidis pheromone. Wherein the allosteric colicin being yielded by artificially mutating the amino acid residues G11A, H22R, A26G, V31L and H40K in the peptide chain of wild type Colicin E1, Ia, Ib, A, B, N, or their ion channel-forming structural domain. In comparison with the traditional antibiotics, the novel antibiotics in the present invention are not likely to lead to drug resistance and cause hypersensitivity reaction.

Abstract: The present invention belongs to field of biology and medicine, and especially relates to a novel antibiotic comprising an antibody mimetic antibody, its preparation methods and uses thereof. A novel antibiotic comprising a antibody mimetic covalently bonded to the carboxyl end of a colicin polypeptide or a channel-forming domain polypeptide of a colicin, wherein said colicin is selected from the group consisting of Colicin E1, Ia, Ib, A, B, N; wherein said antibody mimetic being yielded by fusing two complementarity determining regions (CDRs), VHCDR1 and VLCDR3 through a cognate framework region (VHFR2) of an immunoglobulin; wherein said the immunoglobulin specifically recognizes the bacterial porins. Its antibacterial ability is a thousandfold powerful than normal antibiotics. Due to its unique action mechanism, drug resistance resulted in mutation can hardly be acquired by pathogenic bacteria. And the antibiotic will not hurt normal human cells when it kills pathogenic bacteria.