25 results about "Conformational epitope" patented technology

The invention discloses a chicken infectious anemia subunit vaccine composition as well as a preparation method and application thereof. The vaccine composition contains a mixture of CIAV (Chicken Infectious Anemia Virus) VP1 and VP2 proteins, the mixture of the VP1 and VP2 proteins is prepared by performing in-vitro renaturation on VP1 inclusion body proteins by using a gradient dialysis method, adding pre-purified VP2 proteins in the dialysis process to promote the recovery of key conformation epitopes of the VP1 proteins, and then gradually removing a denaturing agent to obtain the VP1 and VP2 protein mixture. And refolding the VP1 protein to obtain the protein. The soluble VP2 protein is used as a molecular chaperone to recover the VP1 protein from the inclusion body. According to the VP2 protein assisted synergistic refolding strategy, the key conformation epitope of the VP1 protein is recovered by using the natural function of the VP2 protein. Subsequently, the immunogenicity and protective efficacy of the refolded VP1 and VP2 protein mixture are evaluated, and an economic and effective technical means is provided for preventing and controlling chicken infectious anemia.

This invention provides a peanut allergen peptide, its screening method, and its application. Phage display technology is used to screen for conformational epitopes of Ara h5 and Ara h8 proteins. Polyclonal IgE and IgG antibodies against the target proteins are prepared by immunizing BALB / c mice with Ara h5 and Ara h8 proteins as antigens. ELISA and dotted immunoblotting detection revealed that the titers of polyclonal IgG and IgE against Ara h5 and Ara h8 proteins were 1:64000 and 1:320, respectively, and the antibodies exhibited specificity. Using the antibodies as targets, phage display technology screened the conformational epitope sequences of Ara h5 protein as WETIYSR and FHWWYLK. The conformational epitopes of Ara h8 protein were FPYMKFV, FPYMKFR, SMFARID, and SFHWWLF.

The disclosure pertains to conformational epitopes in alpha-synuclein, antibodies thereto and methods of making and using immunogens and antibodies specific thereto. In particular antibodies raised to cyclic compounds comprising at least 3 amino acids of EKTKEQ (SEQ ID NO: 1) selectively recognize misfolded oligomeric alpha-synuclein and are able to inhibit alpha-synuclein propagation and toxicity.

The application provides a PLA2R monoclonal antibody and an ELISA kit comprising the antibody. Specifically, the application provides a monoclonal antibody which specifically binds to PLA2R, wherein the antibody only binds to non-reduced PLA2R antigen with a conformational epitope, does not bind to reduced PLA2R antigen, and does not bind to another antigen THSD7A of primary membranous nephropathy. An ELISA kit prepared based on the antibody can more efficiently and accurately detect primary membranous nephropathy than existing commercial kits.

A monoclonal antibody capable of binding to EV-A71 and the use thereof. The monoclonal antibody has heavy chain complementarity determining regions CDR1-CDR3 as shown in SEQ ID NOs: 1-3 and light chain complementarity determining regions CDR1-CDR3 as shown in SEQ ID NOs: 4-6, can specifically bind to a conformational epitope formed by amino acid at position 159 of structural protein VP2 and amino acid at position 81 of VP3 of EV-A71, thereby blocking the process of virus invasion into a host.

To provide a new method for diagnosing and treating liver cancer.SOLUTION: Provided are isolated antibodies that specifically bind to a conformational epitope of AS-SPIK proteins and do not specifically bind to NS-SPIK proteins, wherein the conformational epitope of the AS-SPIK proteins comprises a specific amino acid sequence of one or more amino acids selected from the group consisting of L14, L15, S16, L17, D24, and S25, and one or more amino acids selected from the group consisting of C58, V59, L60,, and. C61 F62. Methods of producing such antibodies, compositions, such as pharmaceutical compositions, comprising such antibodies, and uses thereof for diagnosing and / or treating disorders characterized by expression of AS-SPIK (e.g., liver cancer) are disclosed. Diagnostic methods and kits containing anti-AS-SPIK antibodies are also disclosed.SELECTED DRAWING: Figure 5

The present invention relates to a method for predicting immunogenic epitopes and an apparatus using the same. The method for predicting immunogenic epitopes according to the present invention includes the steps of: calculating the degree of influence of factors involved in a biological process of a tumor cell for an epitope and characteristics of the epitope on the immunogenicity of the epitope; performing at least one of standardization and normalization on the calculated value; and inputting the value after the standardization and normalization into a pre-trained artificial intelligence model to predict the immunogenicity of the epitope. The biological process may include an antigen processing stage, an antigen presentation stage, an immune stage, and a tumor microenvironment, and the factors involved in the tumor microenvironment may be at least one of an inflammatory response, a B-cell linear epitope, and a B-cell conformational epitope.

The present invention relates to a method for determining the level of PAM and / or its homoisomers and / or fragments thereof in a bodily fluid or tissue sample using an assay comprising at least one binding agent for conformational epitopes of PAM, and to the use of said method for diagnostic purposes.

This invention provides a broad-spectrum non-neutralizing antibody against foot-and-mouth disease virus (FMD) and its application in the preparation of reagents that enhance the production of neutralizing antibodies, belonging to the field of antibody technology. The FMD virus broad-spectrum non-neutralizing antibody has the amino acid sequence of its heavy chain variable region as shown in SEQ ID NO:1 and the amino acid sequence of its light chain variable region as shown in SEQ ID NO:2. This invention utilizes single B-cell antibody technology to screen and obtain a porcine broad-spectrum non-neutralizing monoclonal antibody SP1C6, which can recognize a conformational epitope on VP2. The broad-spectrum non-neutralizing antibody SP1C6 increases the level of neutralizing antibodies induced by FMD virus in pigs by blocking the non-neutralizing epitopes of the FMD virus antigen.

The invention belongs to the technical field of biology, and relates to an anti-AAV6 antibody and application thereof in AAV6 titer determination. The anti-AAV6 monoclonal antibody 3G8 with high specificity is obtained through mouse immunization and antibody screening, and the antibody can specifically recognize and combine with complete AAV6 virus particles or carrier particles. The mouse Anti-AAV6 monoclonal antibody 3G8 has high serotype specificity, is only combined with AAV6 complete virus particles, and does not react with virus particles of other serotypes such as AAV2, AAV5, AAV8, AAV9 and the like. Meanwhile, conformational epitope dependency is achieved, only the native conformational epitope of the AAV6 capsid is recognized, and VP1 subunits, VP2 subunits and VP3 subunits in a depolymerization state are not combined.

A monoclonal antibody capable of binding to EV-A71 and the use thereof. The monoclonal antibody has heavy chain complementarity determining regions CDR1-CDR3 as shown in SEQ ID NOs: 1-3 and light chain complementarity determining regions CDR1-CDR3 as shown in SEQ ID NOs: 4-6, can specifically bind to a conformational epitope formed by amino acid at position 159 of structural protein VP2 and amino acid at position 81 of VP3 of EV-A71, thereby blocking the process of virus invasion into a host.

The application discloses a method for reducing the allergenicity of tenebrio molitor by ultrasonic and enzymatic hydrolysis, and relates to the technical field of food processing and food safety. First, the tenebrio molitor protein is extracted by an alkali solution method, and then the tenebrio molitor protein solution is treated by ultrasonic and enzymatic hydrolysis to change the conformational epitope and linear epitope of the tenebrio molitor protein, and finally, the treated tenebrio molitor protein solution is freeze-dried to obtain tenebrio molitor protein powder with low allergenicity. The ultrasonic cavitation effect and the specific hydrolysis of enzymatic hydrolysis are used to produce a synergistic effect, and under the combined treatment of 300 W ultrasonic power and alkaline protease, the allergenicity reduction rate can reach more than 70%, which is significantly better than single processing mode, and provides technical support for the development of tenebrio molitor low allergenic food.

The invention provides a PLA2R monoclonal antibody and an ELISA (Enzyme-Linked Immunosorbent Assay) kit containing the PLA2R monoclonal antibody. Specifically, the invention provides a monoclonal antibody capable of being combined with PLA2R with high specificity, and the antibody is only combined with a non-reduced PLA2R antigen with conformational epitopes, is not combined with a reduced PLA2R antigen, and is not combined with another antigen THSD7A of primary membranous nephropathy. Compared with an existing commercial kit, the ELISA kit prepared based on the antibody can more efficiently and accurately detect the primary membranous nephropathy.

The present invention is directed to methods for determining the level of PAM and / or its isoforms and / or fragments thereof in a bodily fluid or a tissue sample using an assay, wherein said assay is comprising at least one binder that is directed to a conformational epitope of PAM, and its use for diagnostic purpose.

This invention discloses an active immunization animal model of neuromyelitis optica spectrum disorder and its construction method. The construction method includes: extracting a membrane protein retaining the native conformational epitope of AQP4 from cells overexpressing AQP4-M23 as an immunogen; emulsifying the immunogen with an adjuvant and then actively immunizing non-human mammals to induce the production of autoantibodies against the AQP4 conformational epitope, thereby constructing an active immunization animal model of neuromyelitis optica spectrum disorder. This invention uses an AQP4 membrane protein rich in conformational epitopes as an immunogen, overcoming the limitation of traditional linear peptides in inducing pathogenic autoantibodies in wild-type mice. It successfully constructs an active immunization animal model capable of mimicking the core pathological features of human neuromyelitis optica spectrum disorder (including AQP4 loss and astrocyte damage), providing an important experimental platform for research on the pathogenesis of neuromyelitis optica spectrum disorder and drug screening.

The present invention relates to a method for the treatment of pain, such as hyperalgesia or hyperalgesia, more particularly opioid-induced pain, such as opioid-induced chronic migraine, opioid-induced hyperalgesia (OIH) and opioid-induced hyperalgesia (OIA), the method is performed by administering an antibody and / or antigen-binding fragment thereof having binding specificity for PACAP. The antibodies and / or antigen-binding fragments thereof may comprise sequences of the VH, VL and CDR polypeptides described herein, as well as polynucleotides encoding the same. The antibodies and / or antigen-binding fragments thereof described herein bind to the same linear or conformational epitope on human PACAP as the anti-PACAP antibody, and / or compete to bind to the same linear or conformational epitope on human PACAP as the anti-PACAP antibody.

The disclosure pertains to conformational epitopes in alpha-synuclein, antibodies thereto and methods of making and using immunogens and antibodies specific thereto. In particular antibodies raised to cyclic compounds comprising at least 3 amino acids of EKTKEQ (SEQ ID NO: 1) selectively recognize misfolded oligomeric alpha-synuclein and are able to inhibit alpha-synuclein propagation and toxicity.

The present application relates to a method for extracting epitopes effective in the prevention or treatment of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the method comprising the steps of: (a) extracting, from an anti-spike antibody database, first structural data including known structures and second structural data including unknown structures, and extracting, from a SARS-CoV-2 proteome database, third structural data including known structures; (b) carrying out 3D modeling on the second structural data, and classifying the third structural data into a first group including structural proteins and a second group including both structural proteins and non-structural proteins; (c) carrying out spike-antibody docking on the basis of the first group and the second structural data on which 3D modeling has been carried out; (d) constructing a spike-antibody database on the basis of the first structural data and the docked data, and predicting conformational epitopes on the basis of the second group; (e) characterizing epitopes on the basis of the spike-antibody database and the conformational epitopes; and (f) selecting final epitopes on the basis of analysis results.

The invention provides a peanut allergen polypeptide as well as a screening method and application thereof. And screening conformational epitopes of Ara h 5 and Ara h 8 proteins by using a phage display technology. The Ara h 5 protein and the Ara h 8 protein are used as antigens to immunize BALB / c mice to prepare polyclonal IgE and IgG antibodies of anti-target protein. ELISA (enzyme-linked immuno sorbent assay) and dot immunoblotting detection show that the titers of anti-Ara h 5 and anti-Ara h 8 protein polyclone IgG and anti-Ara h 8 protein polyclone IgE are 1: 64000 and 1: 320 respectively, and the antibody has specificity. The antibody is taken as a target spot, and the conformational epitope sequences of the Ara h 5 protein, which are screened by a phage display technology, are WETIYSR and FHWWYLK. And the conformational epitopes of the Ara h 8 protein are FPYMKFV, FPYMKFR, SMFARID and SFHWWLF (Small Form of Horse and White White Link Factor).

The present disclosure is directed to binding proteins to the extracellular domain (ECD) of HER2 / ErbB2. More particularly, the binding proteins bind to a conformational epitope which is exposed in cells in response to HER2 amplification or activation.

The present invention relates to a method for selecting lymphocytes recognizing a conformational epitope of a protein antigen from a population of cells, comprising a step of identifying at least one lymphocyte binding to at least two separate peptides comprising sequences of the protein antigen, in particular at least three separate peptides comprising sequences of the protein antigen.

The present invention is directed to antibodies and antigen binding fragments thereof having binding specificity for PACAP. The antibodies and antigen binding fragments thereof comprise the sequences of the VH, VL, and CDR polypeptides described herein, and the polynucleotides encoding them. Antibodies and antigen binding fragments described herein bind to and / or compete for binding to the same linear or conformational epitope(s) on human PACAP as an anti-PACAP antibody. The invention contemplates conjugates of anti-PACAP antibodies and binding fragments thereof conjugated to one or more functional or detectable moieties. Methods of making said anti-PACAP antibodies and antigen binding fragments thereof are also contemplated. Other embodiments of the invention contemplate using anti-PACAP antibodies, and binding fragments thereof, for the diagnosis, assessment, and treatment of diseases and disorders associated with PACAP and conditions where antagonism of PACAP-related activities, such as vasodilation, photophobia, mast cell degranulation, and / or neuronal activation, would be therapeutically beneficial.

The invention provides preparation and application of a monoclonal antibody for diagnosis aiming at a human neutrophil lipocalin (HNL) neoepitope. Two new HNL protein conformational epitopes and a new HNL linear epitope are designed and provided, and the anti-HNL antibody which is combined with the new epitopes and has higher binding affinity and better binding specificity is obtained through screening. The anti-HNL antibody disclosed by the invention can be used for preparing an HNL detection reagent and a kit, has higher sensitivity and specificity when being used for detecting HNL protein in a sample, and can be applied to distinguishing bacterial infection and virus infection.

The present invention relates to antibodies that specifically bind to a conformational epitope of human C5a. The invention particularly relates to humanized anti-C5a antibodies. The antibodies described herein are useful as active agents in pharmaceutical compositions. The antibodies and pharmaceutical compositions are especially useful for the treatment and prevention of diseases or disorders involving pathological C5a activity.

The present invention provides a method for identifying a conformational epitope of a protein antigen formed from at least two different peptides comprising sequences from the protein antigen, comprising the steps of: - selecting at least one first peptide comprising a sequence from the protein antigen that is recognized by at least one composition comprising antibodies or antibody-bearing B lymphocytes from at least one individual immunized against the protein antigen; and -3·10 from the first peptide in the three-dimensional structure of the protein antigen -9 selecting at least one second peptide located at a distance of 1 m or less and comprising a sequence from the protein antigen recognized by at least one composition comprising antibodies or antibody-bearing B lymphocytes from at least one individual immunized against the protein antigen of the previous step; Including, The method relates to a method wherein the at least one first peptide and the at least one second peptide form a conformational epitope of a protein antigen.