59 results about "Ige binding epitopes" patented technology

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE-binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than-within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

The present invention relates to methods and compositions designed for the treatment, management, or prevention of cancer, particularly, metastatic cancer. In one embodiment, the methods of the invention comprise the administration of an effective amount of an antibody that binds to EphA2 and agonizes EphA2, thereby increasing EphA2 phosphorylation and decreasing EphA2 levels. In other embodiments, the methods of the invention comprise the administration of an effective amount of an antibody that binds to EphA2 and inhibits cancer cell colony formation in soft agar, inhibits tubular network formation in three-dimensional basement membrane or extracellular matrix preparation, preferentially binds to an EphA2 epitope that is exposed on cancer cells but not non-cancer cells, and / or has a low Koff, thereby, inhibiting tumor cell growth and / or metastasis. The invention also provides pharmaceutical compositions comprising one or more EphA2 antibodies of the invention either alone or in combination with one or more other agents useful for cancer therapy.

The present invention relates to methods and compositions designed for the treatment, management, or prevention of cancer, particularly, metastatic cancer. In one embodiment, the methods of the invention comprise the administration of an effective amount of an antibody that binds to EphA2 and agonizes EphA2, thereby increasing EphA2 phosphorylation and decreasing EphA2 levels. In other embodiments, the methods of the invention comprise the administration of an effective amount of an antibody that binds to EphA2 and inhibits cancer cell colony formation in soft agar, inhibits tubular network formation in three-dimensional basement membrane or extracellular matrix preparation, preferentially binds to an EphA2 epitope that is exposed on cancer cells but not non-cancer cells, and / or has a low Koff, thereby, inhibiting tumor cell growth and / or metastasis. The invention also provides pharmaceutical compositions comprising one or more EphA2 antibodies of the invention either alone or in combination with one or more other agents useful for cancer therapy.

It has been determined that allergens, which are characterized by both humoral (IgE) and cellular (T cell) binding sites, can be modified to be less allergenic by modifying the IgE binding sites. The IgE binding sites can be converted to non-IgE binding sites by masking the site with a compound that prevents IgE binding or by altering as little as a single amino acid within the protein, most typically a hydrophobic residue towards the center of the IgE-binding epitope, to eliminate IgE binding. The method allows the protein to be altered as minimally as possible, other than-within the IgE-binding sites, while retaining the ability of the protein to activate T cells, and, in some embodiments by not significantly altering or decreasing IgG binding capacity The examples use peanut allergens to demonstrate alteration of IgE binding sites. The critical amino acids within each of the IgE binding epitopes of the peanut protein that are important to immunoglobulin binding have been determined. Substitution of even a single amino acid within each of the epitopes led to loss of IgE binding. Although the epitopes shared no common amino acid sequence motif, the hydrophobic residues located in the center of the epitope appeared to be most critical to IgE binding.

The present invention provides a polypeptide having the formula: St-R1-S1-Q-S2-R2 wherein St is a stalk sequence which, when the polypeptide is expressed at the surface of a target cell, causes the R and Q epitopes to be projected from the cell surface; R1 and R2 are a Rituximab-binding epitopes each having the an amino acid sequence selected from the group consisting of SEQ ID No. 1, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 and 16 or a variant thereof which retains Rituximab-binding activity; S1 and S2 are optional spacer sequences, which may be the same or different; and Q is a QBEnd1O-binding epitope having the amino acid sequence shown as SEQ ID No. 2 or a variant thereof which QBEnd1O-binding activity. The invention also provides a nucleic acid sequence encoding such a polypeptide and uses thereof in adoptive cell transfer.

The invention relates to a tetrameric polypeptide comprising a first polypeptide chain comprising a first VL antigen binding domain and a first CL constant domain, a second polypeptide chain comprising a first VH antigen binding domain, a first CH1 constant domain, a first CH2 constant domain and a first CH3 constant domain, a first ligand binding to a HER2 D4 epitope linked to the N-terminus of said first VL antigen binding domain or said first VH antigen binding domain by a first interdomain amino acid linker, a third polypeptide chain comprising a second VL antigen binding domain and a second CL constant domain, a fourth polypeptide chain comprising a second VH antigen binding domain, a second CH1 constant domain, a second CH2 constant domain and a second CH3 constant domain and a third ligand binding to a HER2 D4 epitope linked to the N-terminus of said second VL antigen binding domain or said second VH antigen binding domain by a second interdomain amino acid linker, wherein the VL antigen binding domains and the VH antigen binding domains together constitute a second ligand and a fourth ligand binding to a HER2 D1 epitope. The invention further relates to the tetrameric polypeptide for use in a method for the prevention or treatment of a malignant neoplastic disease, an isolated nucleic acid and a host cell for expression of the polypeptide and a method for obtaining the polypeptide.

High affinity antibodies for binding epitopes of BoNT / B and hybridomas that produce such antibodies are described. The antibodies may be used in a kit for detecting BoNT / B in a sample.

The present disclosure is directed recombinant T cell receptors capable of binding an NY-ESO-1 epitope and nucleic acid molecules encoding the same. In some embodiments, the nucleic acid molecules further comprise a second nucleotide sequence, wherein the second nucleotide sequence or the polypeptide encoded by the second nucleotide sequence inhibits the expression of an endogenous TCR. Other aspects of the disclosure are directed to vectors comprising the nucleic acid molecule and cells comprising the recombinant TCR, the nucleic acid molecule, or the vector. Still other aspects of the disclosure are directed to methods of using the same. In some embodiments, the methods comprise treating a cancer in a subject in need thereof.

The present invention provides systems and methods for preparing and purifying target molecules present in biological systems. Systems and methods according to the present invention utilize a transgenically expressed multivalent binding polypeptide as an affinity medium for purifying the target molecule to purify the target molecule. The transgenic multivalent binding polypeptide binds both the target molecule (eg, a bindable epitope of the target molecule) and the matrix.

The invention relates to a monoclonal antibody capable of neutralizing CYR61 and applications thereof and a hybrid tumor capable of generating the monoclonal antibody. The technical scheme adopted by the invention relates to the monoclonal antibody secreted by the mouse anti-human CYR61 monoclonal antibody hybrid tumor CGMCC No.2766 or CGMCC No.2767, and the applications of the monoclonal antibody to preparation of a medicament for treating rheumatic disease, wherein the rheumatic disease is the chronic infectious arthritis. The invention has the advantages that: (1) the self-prepared monoclonal antibody can research pathogenesis of CYR61 in rheumatoid arthritis and can accurately position the expression of CYR61 and detect the CYR61 level of the blood serum and the lesion sites (such as joints); (2) the monoclonal antibody can be used for preparing a detection kit so as to distinguish clinical diagnostics of osteoarthritis and rheumatoid arthritis; and (3) the monoclonal antibody also can search the combination epitope where the CYR61 on the surface of the synovium and in the synovial of the rheumatoid arthritis patient can be neutralized, and provides the screening basis for preparing a humanized antibody which can neutralize the CYR61 in the next step.

The present disclosure relates to recombinant T cell receptors capable of binding to MAGE-A2 epitopes and nucleic acid molecules encoding the recombinant T cell receptors. In some aspects, the nucleic acid molecule further comprises a second nucleotide sequence, where the second nucleotide sequence or a polypeptide encoded by the second nucleotide sequence inhibits expression of an endogenous TCR. Other aspects of the disclosure relate to a vector comprising the nucleic acid molecule and a cell comprising the recombinant TCR, the nucleic acid molecule, or the vector. Other aspects of the disclosure relate to methods of using the recombinant TCRs, the nucleic acid molecules, the vectors, and the cells. In some aspects, the methods include treating cancer in a subject in need thereof.

The present disclosure relates to recombinant T cell receptors capable of binding to CCND1 epitopes and nucleic acid molecules encoding the recombinant T cell receptors. In some aspects, the nucleic acid molecule further comprises a second nucleotide sequence, where the second nucleotide sequence or a polypeptide encoded by the second nucleotide sequence inhibits expression of an endogenous TCR. Other aspects of the disclosure relate to a vector comprising the nucleic acid molecule and a cell comprising the recombinant TCR, the nucleic acid molecule, or the vector. Other aspects of the disclosure relate to methods of using the recombinant TCRs, the nucleic acid molecules, the vectors, and the cells. In some aspects, the methods include treating cancer in a subject in need thereof.

The invention discloses a monoclonal antibody 5E9 against Ebola virus glycoprotein GP1 subunit, the antibody has a unique CDR region, has good binding activity with EBOV GP, EC 50 The value is 0.006 μg / mL. Compared with the control antibody, 5E9 can effectively neutralize the EBOV pseudovirus in vitro, and its neutralizing activity increases with the increase of antibody concentration. At a concentration of 1 μg / mL, it can achieve 100% neutralization of EBOV pseudovirus-infected cells. %protection of. 5E9 also has good neutralizing activity against EBOV in vitro, and can be used as a candidate therapeutic drug for Ebola virus disease. The binding epitope of 5E9 is located at amino acid 95-190 of the GP antigen, which is different from neutralizing antibodies in the prior art. It has the potential to form a cocktail combination therapy with other neutralizing antibodies.

The invention discloses a multi sub-gene resistant type HCV (Hepatitis C Virus) antibody gene R3-19, wherein the heavy chain amino acid sequence thereof is shown by SEQ ID NO.38, and the light chain amino acid sequence is shown by SEQ ID NO.39, the antibody gene is obtained by vanning in an independently-constructed anti-HCV scFv antibody library through E2 region aa412-423 linear epitope (an HCV CD81 receptor binding epitope) synthetic peptide which is highly conservative in various subtype HCVs; the antibody library is formed by 39 parts of anti-HCV antibody positive peripheral blood samples of Chinese patients, the HCVs infected by the patients cover the main HCV popular subtypes in China, therefore, the R3-19 is an anti-HCV antibody which is typical in China and has wide binding characteristic, and has excellent application value in the fields of HCV diagnosis, HCV treatment, vaccine research and development and the like in China.