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15 results about "Antibody hypervariable region" patented technology
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In antibodies, hypervariable regions form the antigen-binding site and are found on both light and heavy chains. They also contribute to the specificity of each antibody. In a variable region, the 3 HV segments of each heavy or light chain fold together at the N-terminus to form an antigen binding pocket.
This invention relates to the field of bioengineering technology, specifically to a recombinant adenovirus displaying a large antigen fragment on its capsid surface, its construction method, and its applications. The HVR1 and HVR5 regions of the hexon hypervariable region of this virus are replaced by gene fragments containing exogenous genes; each exogenous gene fragment has a flexible linker attached to both ends, and the gene sequence of the flexible linker is shown in SEQ ID No. 1. By precisely locating the naturally variable HVR1 and HVR5 loop regions exposed on the surface of the hexon protein as insertion sites, and supplementing them with flexible linkers, the core problem of exogenous sequence insertion disrupting the stability of the hexon structure is successfully solved. This allows for stable packaging to produce viral particles with high titers and infectivity, enabling the development of a new generation of highly efficient and safe capsid-displaying adenovirus vaccines.
The invention discloses a strain identification method based on a 16S rRNA (ribosomal Ribonucleic Acid) hypervariable region. According to the invention, a plurality of hypervariable regions of 16S rRNA are integrated, the distinguishing ability of specific strains in different variable regions and other strains belonging to the same genus is researched through a molecular evolutionary tree method, and finally, the combination of different hypervariable regions can be found, so that the purpose of identifying the specific strains at the species level is achieved.
The invention provides a sheep-derived component rapid quantitative detection method based on dual real-time fluorescent PCR. According to the method, a single-copy nuclear gene GAPDH is taken as a target spot, a sheep specific primer and a probe are designed in a hypervariable region of the single-copy nuclear gene GAPDH, and an internal reference primer and a probe capable of identifying various common animal-derived components are designed in a conserved region of the single-copy nuclear gene GAPDH. As the target and the internal reference are located in the same gene and coexist in the same cell according to the proportion of 1: 1, quantitative deviation caused by gene copy number difference or expression fluctuation in a traditional two-step method is remarkably reduced. The detection strategy constructed by the invention has double advantages of specific recognition and broad-spectrum reference, is clear in quantitative basis and simple and convenient to operate, is suitable for rapid recognition and quantitative adulteration analysis of sheep-derived components in meat products, and has wide application prospects and supervision values.
The invention discloses an Ad4-55 / Ad7-3 type tetravalent recombinant adenovirus vaccine and an application of the Ad4-55 / Ad7-3 type tetravalent recombinant adenovirus vaccine. The preparation method comprises the following steps: replacing a fifth hypervariable region of an HAdV-4 hexon in an HAdV-4 genome with a second hypervariable region of an HAdV-55 hexon to obtain a recombinant adenovirus Ad4-55; and replacing the first hypervariable region of the HAdV-7 hexon in the HAdV-7 genome with the first hypervariable region of the HAdV-3 hexon, so as to obtain the recombinant adenovirus Ad7-3. And mixing the recombinant adenovirus Ad4-55 and the recombinant adenovirus Ad7-3 to obtain the tetravalent recombinant adenovirus vaccine. Experiments prove that when the tetravalent recombinant adenovirus vaccine prepared by the invention is used for immunizing mice, high-level specific IgG antibodies and neutralizing antibodies can be induced. According to the present invention, the important application value is provided for the prevention and control of HAdV-3, HAdV-7, HAdV-4 and HAdV-55.
The present invention provides a library containing synthetic polynucleotides encoding antibody heavy chains (e.g., heavy chains of dynamic human antibodies), as well as antibody heavy chains, antibodies, cells, animals, methods, and kits related thereto. [Solution] Provided herein is a library containing polynucleotides, one of which encodes an antibodyheavy chain containing specific hypervariable regions HVR-H1 and HVR-H2. Further provided herein is a library containing polynucleotides encoding a plurality of unique antibodies, each antibody containing a heavy chain variable region and a light chain variable region. Also provided relating to the antibodies, polypeptide libraries, vector libraries, cells, non-human animals, antibody heavy chains, methods for constructing antibody libraries, kits, and methods for producing bispecific antibodies.
This invention relates to the field of biological protein application technology, and discloses the application of flagellinhypervariable region H as an intramolecular adjuvant in vaccine preparation. The amino acid sequence of flagellinhypervariable region H is shown in SEQ ID NO.3, and the nucleotide sequence of the gene encoding flagellinhypervariable region H is shown in SEQ ID NO.4. This invention also discloses an expression cassette, recombinant vector, recombinant cells, or recombinant bacteria containing the gene encoding flagellin hypervariable region H. This invention uses the aforementioned flagellin hypervariable region H as an intramolecular adjuvant in vaccine preparation. This invention connects flagellin hypervariable region H to an antigenic epitope to obtain a fusion protein. Compared with existing technologies, the solubility and activity of the fusion protein are improved. Simultaneously, this invention overcomes the expression form of inclusion bodies in existing E. coli expression systems, eliminating the need for subsequent refolding and assembly, thus simplifying the vaccine preparation process.