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112results about How to "Maintain immunogenicity" patented technology

Recombinant bacillus displaying GCRV VP7 proteins on surface of bacillus subtilis GC5 and preparation method

The invention discloses a recombinant bacillus displaying GCRV VP7 proteins on the surface of bacillus subtilis GC5 and a preparation method. The preparation method comprises the following steps: (1) obtaining a present epidemic strain type-II GCRV VP7 nucleotide sequence; (2) separating wide bacillus from the body of a grass carp, determining the wide bacillus to be bacillus subtilis, and naming the wide bacillus as Bacillus subtilis GC5, CCTCC NO: M2014654; (3) constructing a fusion expression recombinant integrated carrier, wherein a vp7 sequence in recombinant plasmids is the nucleotide sequence shown in SEQ ID No. 1; (4) preparing and authenticating recombinant bacillus subtilis, CCTCC NO: M2014655; (5) inducing and authenticating the recombinant bacillus displaying VP7 on the surface. The generation rate of spores is up to 100%, and the recombinant bacillus is simple and convenient to produce, low in cost, and capable of being used as a feed additive; the recombinant bacillus has an intestinal customization capacity, as well as is beneficial to regulating the intestinal bacterial colony balances of animals, improving the body immunocompetence of the animals, and enhancing the nutrition metabolism functions of the animals. The spores are high in stress resistance and easy for large-scale production, as well as solve the problem of instability of GCRV VP7 proteins used as immunizing antigens in extreme environments.
Owner:INST OF AQUATIC LIFE ACAD SINICA

Building method for autovaccine by aiming at human TNF(Tumor Necrosis Factor)-alpha molecule

InactiveCN102370979AMaintain immunogenicityRemove natural biological activityBacteriaAntipyreticL929 cellEscherichia coli
The invention discloses a building method for autovaccine in-vivo induced by aiming at human TNF(Tumor Necrosis Factor)-alpha molecule. With a step-by-step cloning method, a fusion gene of hTNF-TT830-844, hTNF-HEL46-61 and hTNF-PADRE is built; point mutation (T439-A,C440-G) is introduced into a natural human TNF gene to optimize a mRNA (Ribonucleic Acid) secondary structure; the fusion gene is cloned into a pET22b prokaryotic expression vector, and efficient expression is achieved in the bacterial strain of escherichia coli; three T accessory cell epitope peptides are introduced between the epitope peptide structure domains of hTNF by the computer-aided analysis and is fused with the hTNF-alpha to overcome the immunological tolerance of an organism for the autologous protein, and therefore the organism generates high-level humoral immune response; the generated high-level hTNF-alpha neutralizing polyclone antibody can neutralize killing activity of the hTNF-alpha on L929 cells in vitro; the hTNF-PADRE has the strongest immunogenicity; the high-level antibody can be induced under the condition of using no immunological adjuvant; and the vaccine has favorable protection and curing action on mouse models suffering from rheumatoid arthritis induced by the II-type collagen, cachexia and the like induced by LPS (lipopolysaccharide).
Owner:FOURTH MILITARY MEDICAL UNIVERSITY

Acinetobacter baumannii zinc dependent oligopeptide A1S-1610 recombinant protein and preparation method and application thereof

The invention relates to an acinetobacter baumannii A1S-1610 protein, a carrier, engineering bacteria, a composition or a kit which comprises the acinetobacter baumannii 1 A1S-1610 protein, and a preparation method and application of the acinetobacter baumannii 1 A1S-1610 protein, the acinetobacter baumannii 1 A1S-1610 protein is never used in the field of recombinant subunit vaccines, the acinetobacter baumannii 1 A1S-1610 protein can effectively stimulate the body to cause a protective immune response so as to resist acinetobacter baumannii lethal infection. The present invention also discloses a method for preparation of the recombinant protein by construction of an expression vector of the recombinant protein, and transformation of host bacteria, and use of the recombinant protein in the preparation of an acinetobacter baumannii resistant subunit vaccine and a related detection kit. The protective antigen composition A1S_1610 protein is expressed by use genetic engineering technology to clone, and the A1S_1610 protein is high in expression amount, easy to separate and purify, efficient and safe, and the genetic engineering recombinant subunit vaccine has good acinetobacter baumannii infection resistant immune protection effect.
Owner:ARMY MEDICAL UNIV

Clostridium perfringens Beta toxin recombination subunit vaccine and production method thereof

ActiveCN109078178AEfficient expressionEfficient soluble expressionAntibacterial agentsBacterial antigen ingredientsClostridium perfringens beta toxinVaccine Production
The invention relates to a clostridium perfringens Beta toxin recombination subunit vaccine and a production method thereof. The prepared clostridium perfringens Beta toxin recombination subunit vaccine is produced by using a recombination clostridium perfringens Beta toxin protein which is processed by codon optimization and contains 4 amino acid mutations, namely integrity and spatial conformation of a natural toxin protein are reserved in the greatest degree, so immunogenicity of the natural toxin protein is kept, and a biological potential safety hazard caused by the single amino acid mutation is avoided. The vaccine further has the advantages of simple preparation process, low immunizing dose, good vaccine efficacy and the like. Compared with a current commercial clostridium perfringens natural toxin inactivated vaccine in China, a bio-safety risk in a vaccine production process is greatly reduced. The vaccine is a perfect candidate vaccine for updating a current C-type clostridium perfringens toxin vaccine in China. In addition, while a mixed vaccine is prepared by the vaccine with other antigens, the mixed vaccine can be prepared without increasing a using dose of the mixedvaccine.
Owner:CHINA INST OF VETERINARY DRUG CONTROL

Recombinant protein of methicillin-resistant staphylococcus aureus IsdB protein active segment, preparation method thereof and application thereof

The invention discloses a recombinant protein of active segment IsdB2 of decision protein IsdB on the surface of methicillin-resistant staphylococcus aureus iron ion, wherein the amino acid sequence of the recombinant protein is SEQ ID No: 3 or the sequence which has the same or similar function as the SEQ ID No: 3 obtained by adding or deleting a plurality of amino acids at the amino terminal and/or the carboxyl terminal of the SEQ ID No: 3. The invention further discloses a method for preparing the recombinant protein by building the expression vector of the recombinant protein and transforming the host bacteria, and the use of the recombinant protein in the aspect of preparing the subunit vaccine and the related assay kits resisting the methicillin-resistant staphylococcus aureus. By adopting the gene engineering technology, in the invention, the truncated protective antigens component IsdB2 is expressed by cloning through the protein expressing, thereby being high in expression index, convenient to separate and purify, and high-efficiency and safe. Due to the gene engineering, the recombinant polyvaccine has good immune protective effect on resisting the MRSA (methicillin-resistant staphylococcus aureus) infection.
Owner:CHONGQING YUANLUN BIOTECH +1

Building method for autovaccine by aiming at human TNF(Tumor Necrosis Factor)-alpha molecule

InactiveCN102370979BMaintain immunogenicityRemove natural biological activityBacteriaAntipyreticEscherichia coliL929 cell
The invention discloses a building method for autovaccine in-vivo induced by aiming at human TNF(Tumor Necrosis Factor)-alpha molecule. With a step-by-step cloning method, a fusion gene of hTNF-TT830-844, hTNF-HEL46-61 and hTNF-PADRE is built; point mutation (T439-A,C440-G) is introduced into a natural human TNF gene to optimize a mRNA (Ribonucleic Acid) secondary structure; the fusion gene is cloned into a pET22b prokaryotic expression vector, and efficient expression is achieved in the bacterial strain of escherichia coli; three T accessory cell epitope peptides are introduced between the epitope peptide structure domains of hTNF by the computer-aided analysis and is fused with the hTNF-alpha to overcome the immunological tolerance of an organism for the autologous protein, and therefore the organism generates high-level humoral immune response; the generated high-level hTNF-alpha neutralizing polyclone antibody can neutralize killing activity of the hTNF-alpha on L929 cells in vitro; the hTNF-PADRE has the strongest immunogenicity; the high-level antibody can be induced under the condition of using no immunological adjuvant; and the vaccine has favorable protection and curing action on mouse models suffering from rheumatoid arthritis induced by the II-type collagen, cachexia and the like induced by LPS (lipopolysaccharide).
Owner:FOURTH MILITARY MEDICAL UNIVERSITY

Preparation method of chicken infectious bronchitis N-2-hydroxypropyl trimethyl ammonium chloride chitosan/carboxymethyl chitosan nano living vaccine

The invention provides a preparation method of a chicken infectious bronchitis N-2-hydroxypropyl trimethyl ammonium chloride chitosan / carboxymethyl chitosan nano living vaccine and relates to a preparation method of a chicken infectious bronchitis nano living vaccine. The invention aims at providing the preparation method of chicken infectious bronchitis N-2-hydroxypropyl trimethyl ammonium chloride chitosan / carboxymethyl chitosan nano living vaccine. The preparation method comprises the following steps of: firstly, preparing a virus solution and adding the virus solution into an N-2-hydroxypropyl trimethyl ammonium chloride chitosan solution after filtration sterilization, and stirring to obtain a mixed solution A; secondly, dropwise adding a carboxymethyl chitosan solution into the mixed solution A after filtration sterilization to obtain a mixed solution B; thirdly, centrifuging the mixed solution B, then washing sediments with sterile deionized water at the temperature of 4 DEG C for three times, and collecting solid-phase materials; and fourthly, adding the solid-phase materials into the sterile deionized water at the temperature of 4 DEG C, then adding 5% of cane sugar skimmed milk solution, and then carrying out vacuum freeze drying, thus the preparation method is completed. The preparation method provided by the invention is applied to the field of veterinary drugs.
Owner:HEILONGJIANG UNIV

Preparation method of Burkholderia pseudomallei recombined BLF1 protein, product prepared through preparation method and application of Burkholderia pseudomallei recombined BLF1 protein

The invention discloses a preparation method of Burkholderia pseudomallei recombined BLF1 protein, the product prepared through the preparation method and an application of the Burkholderia pseudomallei recombined BLF1 protein. The preparation method includes the steps that a primer for amplifying a Burkholderia pseudomallei BLF1 gene is designed firstly, a sequence shown in SEQ ID NO.3 of a coding area sequence is obtained through amplification, then the acquired sequence is connected to an expression vector to construct a recombinant expression vector, the recombinant expression vector is converted into host bacteria, and through inducible expression, the Burkholderia pseudomallei recombined BLF1 protein is obtained. The preparation method is simple, the space design conception and immunogenicity of the purified protein can be kept to the maximum degree, the purity of the protein is larger than 95%, it is proved through a mouse experiment that the purified protein has animal toxicity, it is shown that the purified protein has biological activity, the purified protein acts on A549 cells, cell growth can be restrained, and thus the Burkholderia pseudomallei recombined BLF1 protein can be used for preparing anti-tumor medicine and has wide application prospects.
Owner:THE FIRST AFFILIATED HOSPITAL OF THIRD MILITARY MEDICAL UNIVERSITY OF PLA
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