43 results about "Conformational epitope" patented technology

The invention belongs to the field of biology, and discloses a foot-and-mouth disease virus O-type inner broad-spectrum neutralizing swine monoclonal antibody and application thereof, the amino acid sequence of a heavy chain variable region of the monoclonal antibody is shown as SEQ ID NO.1, the amino acid sequence of a light chain variable region of the monoclonal antibody is shown as SEQ ID NO.2, the antigen key amino acid residue recognized by the monoclonal antibody is VP2 protein 77 site, and the amino acid sequence of the heavy chain variable region of the monoclonal antibody is shown as SEQ ID NO.1. The amino acid sequence of the light chain variable region of the monoclonal antibody is shown as SEQ ID NO.2. The site is located at a structural protein VP2B-C ring, is a conformational epitope, does not react with an A-type antigen, is an intra-strain broad-spectrum neutralizing antibody, and shows relatively strong neutralizing efficacy (IC50 is less than 5 [mu] g.mL <-1 >). Meanwhile, the invention also provides application of the monoclonal antibody.

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.

The invention relates to a small molecule detection method. The method comprises the following steps: forming a multi-component compound containing'a first compound antibody-small molecules / small molecule binding partner compound-a second compound antibody ', and detecting the small molecules in a sample by detecting the multi-component compound, the micromolecule binding partner can be specifically bound with micromolecules, has at least two antigen binding sites, and can be bound with at least two micromolecules to obtain the micromolecule / micromolecule binding partner compound. And forming at least two new conformational epitopes different from the small molecule in the free state and the small molecule binding partner in the free state; each of the first complex antibody and the second complex antibody specifically binds to at least one new conformational epitope, and neither the first complex antibody nor the second complex antibody is an antibody of the small molecule antigen nor a specific antibody of the small molecule binding partner.

The present invention belongs to the field of antibody technology, and specifically relates to anti-herpes zoster virus glycoprotein E monoclonal antibodies and binding epitope analysis methods. VZV gE protein is used as an immunogen to immunize mice, determine the protein titer, perform fusion experiments, and subclone experiments to obtain monoclonal antibodies. The analysis method is as follows: determine that the antibody recognition epitopes are all conformational epitopes; analyze the complete structure of the VZV gE protein, predict the disulfide bond position and antigenic epitope; mutate and identify the cysteine ​​residues in the VZV gE sequence predicted to form disulfide bonds or affect the formation of disulfide bonds one by one; transfect and express the recombinant mutant plasmid, detect the expression of mutant and wild-type proteins; detect the activity of monoclonal antibodies; detect the activity of monoclonal antibodies corresponding to the mutant proteins with the same expression amount; and detect the affinity of monoclonal antibodies. Application: pharmaceutical composition, reagent, test strip or kit, biological product. The present invention fills the gap in the current analysis of conformational epitopes of VZV gE protein antigens.

The present invention relates to binding proteins of the extracellular domain (ECD) of HER2 / ErbB2. More specifically, binding proteins bind to conformational epitopes exposed in cells that respond to HER2 expansion or activation.

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 invention belongs to the field of biology, and discloses a broad-spectrum neutralizing porcine monoclonal antibody for foot-and-mouth disease virus type O and its application. The amino acid sequence of the heavy chain variable region of the monoclonal antibody is shown in SEQ ID NO.1, and the amino acid sequence of the light chain variable region is shown in SEQ ID NO.2. The key amino acid residue of the antigen recognized by the monoclonal antibody is position 77 of the VP2 protein. The site is located in the VP2B-C loop of the structural protein and is a conformational epitope. The site does not react with type A antigen, is a broad-spectrum neutralizing antibody within the type, and exhibits a strong neutralizing efficacy (IC 50 <5μg·mL ‑1 ). At the same time, the present invention also provides the application of the monoclonal antibody.

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.

To provide an anti-C5a antibody exhibiting superior blockade of C5a activity.SOLUTION: The present invention relates to antibodies that specifically bind to a conformational epitope of human C5a. In particular, it 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 associated with pathological C5a activity.SELECTED DRAWING: None

The invention provides a monoclonal antibody 3G1 capable of specifically recognizing CV-A5 virus and having neutralizing activity and application of the monoclonal antibody 3G1. The monoclonal antibody is prepared from a CV-A5 virus antigen immunized mouse and splenocytes of the mouse through a cell fusion technology, and amino acid sequences of three CDR regions of a heavy chain variable region of the monoclonal antibody sequentially comprise sequences as shown in SEQ ID NO.1-3; the amino acid sequences of the three CDR regions of the light chain variable region sequentially comprise sequences as shown in SEQ ID NO.4-6. The monoclonal antibody can be specifically combined with a CV-A5 virus, and is not combined with enteroviruses such as EV-A71, CV-A10, CV-A6, CV-A16 and the like. The monoclonal antibody targets conformational epitopes, has neutralizing activity, can specifically recognize CV-A5 viruses, is an ideal CV-A5 antigen detection antibody, and is beneficial to acceleration of the research and development process of hand-foot-mouth multivalent vaccines containing CV-A5 pathogens.

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

An object is to provide a novel antibody or antigen-binding fragment thereof against exon 21 of human periostin. The object is achieved by an antibody or antigen-binding fragment thereof bindable to a conformational epitope on human periostin, wherein the epitope contains the amino acid sequence A represented by SEQ ID NO: 61 and the amino acid sequence B represented by any one of SEQ ID NOs: 62 to 64.

The present invention provides a water-soluble rapid immune adjuvant, which comprises 7α,25-OHC, cyclodextrin, aluminum salt, chitosan-based thermosensitive hydrogel and deionized water. When the water-soluble rapid immune adjuvant of the present invention is used, emulsification is not required. After the antigen and the adjuvant are mixed evenly, they are directly injected for immunization in a water-soluble manner, which is convenient to operate and avoids the destruction of the antigen during the emulsification process. Moreover, it will not cause the eversion of hydrophobic groups, retains the natural conformation of the antigen, and can obtain antibodies against conformational epitopes.

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 invention provides a multi-epitope vaccine antigen based on BCG, which comprises a recombinant epitope polypeptide sequence formed by sequentially connecting a CD8 + T cell epitope (CTL) polypeptide sequence, a CD4 + T cell epitope (HTL) polypeptide sequence, a B cell epitope (LBEs) polypeptide sequence and a B cell conformational epitope (CBEs) polypeptide sequence in series, the multi-epitope vaccine antigen provided by the invention can have good recognition and binding effects with an immune related receptor, is an effective immune antigen target, has a relatively strong immune effect, has a remarkable effect on humoral immune level and cellular immune level induced in a mouse body, and is higher than BCG immune level.

The invention provides a monoclonal antibody capable of specifically recognizing a CV-A5 virus and having neutralizing activity and application of the monoclonal antibody. The monoclonal antibody is prepared from a CV-A5 virus antigen immunized mouse and splenocytes of the mouse through a cell fusion technology, and amino acid sequences of three CDR regions of a heavy chain variable region of the monoclonal antibody are sequentially shown as SEQ ID NO.1-3; the amino acid sequences of the three CDR regions of the light chain variable region are sequentially as shown in SEQ ID NO.4-6. The monoclonal antibody can be specifically combined with a CV-A5 virus, and is not combined with enteroviruses such as EV-A71, CV-A10, CV-A6, CV-A16 and the like. The monoclonal antibody targets conformational epitopes, has neutralizing activity, can specifically recognize CV-A5 viruses, is an ideal CV-A5 antigen detection antibody, and is beneficial to acceleration of the research and development process of hand-foot-mouth multivalent vaccines containing CV-A5 pathogens.

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 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 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.

The invention belongs to the technical field of biology, discloses a monoclonal antibody capable of recognizing conformational epitopes and neutralizing porcine acute diarrhea syndrome coronavirus and application of the monoclonal antibody, and particularly discloses an antibody or an antigen binding fragment thereof. The antibody provided by the invention can neutralize 200 SADS-CoV virions of TCID50 under the concentration of 31.75 mu g / mL, the antibody is detected to have very strong affinity with S protein through a BLI test, the antibody is not easy to dissociate after being combined, and an important material is provided for research and development of SADS-CoV neutralizing antibody antiviral drugs.

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.